https://www.cazypedia.org/api.php?action=feedcontributions&feedformat=atom&user=Yaoguang+ChangCAZypedia - User contributions [en-ca]2026-05-05T02:34:44ZUser contributionsMediaWiki 1.35.10https://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18573User:Yaoguang Chang2024-11-04T13:54:24Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] for marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
'''Glycoside Hydrolase'''<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a Zhang2023b</cite><br />
*[[GH95]]: fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2024</cite><br />
*[[GH150]]: λ-carrageenase Cgl150A<br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024d</cite><br />
*[[Multiple GH domain enzymes]]: mannanase Man26/5<cite>Song2024</cite><br />
'''Polysaccharide Lyase'''<br />
*[[PL6]]: alginate lyase Aly6A <cite>Li2024a</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite>, alginate lyase Aly7A <cite>Li2024a</cite>, alginate lyase Aly7Ce <cite>Li2024b</cite>, and alginate lyase Aly7Aq <cite>Li2024c</cite><br />
*[[PL17]]: alginate lyase Aly17A <cite>Li2024a</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
'''Carbohydrate-Binding Module'''<br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite>, AmCBM16 (porphyran-binding CBM) <cite>Mei2024b</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024a</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Zhang2024 pmid=38763726<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024a pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Shen2024d pmid=37940306<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
#Song2024 pmid=38632679<br />
#Li2024a pmid=37540808<br />
#Li2024b pmid=38111122<br />
#Li2024c pmid=39029836<br />
#Mei2024b pmid=38518929<br />
</biblio><br />
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<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18572User:Yaoguang Chang2024-11-04T13:54:01Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] for marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
'''Glycoside Hydrolase'''<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a Zhang2023b</cite><br />
*[[GH95]]: fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2024</cite><br />
*[[GH150]]: λ-carrageenase Cgl150A<br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024d</cite><br />
*[[Multiple GH domain enzymes]]: mannanase Man26/5<cite>Song2024</cite><br />
'''Polysaccharide Lyase'''<br />
*[[PL6]]: alginate lyase Aly6A <cite>Li2024a</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite>, alginate lyase Aly7A <cite>Li2024a</cite>, alginate lyase Aly7Ce <cite>Li2024b</cite>, alginate lyase Aly7Aq <cite>Li2024c</cite><br />
*[[PL17]]: alginate lyase Aly17A <cite>Li2024a</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
'''Carbohydrate-Binding Module'''<br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite>, AmCBM16 (porphyran-binding CBM) <cite>Mei2024b</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024a</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Zhang2024 pmid=38763726<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024a pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Shen2024d pmid=37940306<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
#Song2024 pmid=38632679<br />
#Li2024a pmid=37540808<br />
#Li2024b pmid=38111122<br />
#Li2024c pmid=39029836<br />
#Mei2024b pmid=38518929<br />
</biblio><br />
<br />
<br />
<br />
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<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18571User:Yaoguang Chang2024-11-04T13:47:51Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] for marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
'''Glycoside Hydrolase'''<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a Zhang2023b</cite><br />
*[[GH95]]: fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2024</cite><br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024d</cite><br />
*[[Multiple GH domain enzymes]]: mannanase Man26/5<cite>Song2024</cite><br />
'''Polysaccharide Lyase'''<br />
*[[PL6]]: alginate lyase Aly6A <cite>Li2024a</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite>, alginate lyase Aly7A <cite>Li2024a</cite>, alginate lyase Aly7Ce <cite>Li2024b</cite>, alginate lyase Aly7Aq <cite>Li2024c</cite><br />
*[[PL17]]: alginate lyase Aly17A <cite>Li2024a</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
'''Carbohydrate-Binding Module'''<br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite>, AmCBM16 (porphyran-binding CBM) <cite>Mei2024b</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024a</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Zhang2024 pmid=38763726<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024a pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Shen2024d pmid=37940306<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
#Song2024 pmid=38632679<br />
#Li2024a pmid=37540808<br />
#Li2024b pmid=38111122<br />
#Li2024c pmid=39029836<br />
#Mei2024b pmid=38518929<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18570User:Yaoguang Chang2024-11-04T13:41:38Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] for marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
'''Glycoside Hydrolase'''<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a Zhang2023b</cite><br />
*[[GH95]]: fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2024</cite><br />
*[[GH150]]: λ-carrageenase Cgl150A<br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024d</cite><br />
*[[Multiple GH domain enzymes]]: mannanase Man26/5<cite>Song2024</cite><br />
'''Polysaccharide Lyase'''<br />
*[[PL6]]: alginate lyase Aly6A <cite>Li2024a</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite>, alginate lyase Aly7A <cite>Li2024a</cite>, alginate lyase Aly7Ce <cite>Li2024b</cite>, alginate lyase Aly7Aq <cite>Li2024c</cite><br />
*[[PL17]]: alginate lyase Aly17A <cite>Li2024a</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
'''Carbohydrate-Binding Module'''<br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite>, AmCBM16 (porphyran-binding CBM) <cite>Mei2024b</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024a</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Zhang2024 pmid=38763726<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024a pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Shen2024d pmid=37940306<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
#Song2024 pmid=38632679<br />
#Li2024a pmid=37540808<br />
#Li2024b pmid=38111122<br />
#Li2024c pmid=39029836<br />
#Mei2024b pmid=38518929<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18569User:Yaoguang Chang2024-11-04T13:40:54Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] for marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
'''Glycoside Hydrolase'''<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a Zhang2023b</cite><br />
*[[GH95]]: fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2024</cite><br />
*[[GH150]]: λ-carrageenase Cgl150A<br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024d</cite><br />
*[[Multiple GH domain enzymes]]: mannanase Man26/5<cite>Song2024</cite><br />
'''Polysaccharide Lyase'''<br />
*[[PL6]]: alginate lyase Aly6A <cite>Li2024a</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite>, alginate lyase Aly7A <cite>Li2024a</cite>, alginate lyase Aly7Ce <cite>Li2024b</cite>, alginate lyase Aly7Aq <cite>Li2024c</cite><br />
*[[PL17]]: alginate lyase Aly17A <cite>Li2024a</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite>, AmCBM16 (porphyran-binding CBM) <cite>Mei2024b</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024a</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Zhang2024 pmid=38763726<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024a pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Shen2024d pmid=37940306<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
#Song2024 pmid=38632679<br />
#Li2024a pmid=37540808<br />
#Li2024b pmid=38111122<br />
#Li2024c pmid=39029836<br />
#Mei2024b pmid=38518929<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18568User:Yaoguang Chang2024-11-04T13:40:11Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] for marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
'''Glycoside Hydrolase'''<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a Zhang2023b</cite><br />
*[[GH95]]: fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2024</cite><br />
*[[GH150]]: λ-carrageenase Cgl150A<br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024d</cite><br />
*[[Multiple GH domain enzymes]]: mannanase Man26/5<cite>Song2024</cite><br />
*[[PL6]]: alginate lyase Aly6A <cite>Li2024a</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite>, alginate lyase Aly7A <cite>Li2024a</cite>, alginate lyase Aly7Ce <cite>Li2024b</cite>, alginate lyase Aly7Aq <cite>Li2024c</cite><br />
*[[PL17]]: alginate lyase Aly17A <cite>Li2024a</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite>, AmCBM16 (porphyran-binding CBM) <cite>Mei2024b</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024a</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Zhang2024 pmid=38763726<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024a pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Shen2024d pmid=37940306<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
#Song2024 pmid=38632679<br />
#Li2024a pmid=37540808<br />
#Li2024b pmid=38111122<br />
#Li2024c pmid=39029836<br />
#Mei2024b pmid=38518929<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18567User:Yaoguang Chang2024-11-04T13:35:12Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] for marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a Zhang2023b</cite><br />
*[[GH95]]: fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2024</cite><br />
*[[GH150]]: λ-carrageenase Cgl150A<br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024d</cite><br />
*[[Multiple GH domain enzymes]]: mannanase Man26/5<cite>Song2024</cite><br />
*[[PL6]]: alginate lyase Aly6A <cite>Li2024a</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite>, alginate lyase Aly7A <cite>Li2024a</cite>, alginate lyase Aly7Ce <cite>Li2024b</cite>, alginate lyase Aly7Aq <cite>Li2024c</cite><br />
*[[PL17]]: alginate lyase Aly17A <cite>Li2024a</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite>, AmCBM16 (porphyran-binding CBM) <cite>Mei2024b</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024a</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Zhang2024 pmid=38763726<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024a pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Shen2024d pmid=37940306<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
#Song2024 pmid=38632679<br />
#Li2024a pmid=37540808<br />
#Li2024b pmid=38111122<br />
#Li2024c pmid=39029836<br />
#Mei2024b pmid=38518929<br />
</biblio><br />
<br />
<br />
<br />
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<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18566User:Yaoguang Chang2024-11-04T13:33:43Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] for marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a Zhang2023b</cite><br />
*[[GH95]]: fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2024</cite><br />
*[[GH150]]: λ-carrageenase Cgl150A<br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024d</cite><br />
*[[Multiple GH domain enzymes]]: mannanase Man26/5<cite>Song2024</cite><br />
*[[PL6]]: alginate lyase Aly6A <cite>Li2024a</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite>, alginate lyase Aly7A <cite>Li2024a</cite>, alginate lyase Aly7Ce <cite>Li2024b</cite>, alginate lyase Aly7Aq <cite>Li2024c</cite><br />
*[[PL17]]: alginate lyase Aly17A <cite>Li2024a</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite>, AmCBM16 (Porphyran-binding CBM) <cite>Mei2024b</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024a</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Zhang2024 pmid=38763726<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024a pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Shen2024d pmid=37940306<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
#Song2024 pmid=38632679<br />
#Li2024a pmid=37540808<br />
#Li2024b pmid=38111122<br />
#Li2024c pmid=39029836<br />
#Mei2024b pmid=38518929<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18565User:Yaoguang Chang2024-11-04T13:14:03Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] for marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a Zhang2023b</cite><br />
*[[GH95]]: fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2024</cite><br />
*[[GH150]]: λ-carrageenase Cgl150A<br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024d</cite><br />
*[[Multiple GH domain enzymes]]: mannanase Man26/5<cite>Song2024</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Zhang2024 pmid=38763726<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024 pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Shen2024d pmid=37940306<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
#Song2024 pmid=38632679<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18560User:Yaoguang Chang2024-11-04T02:32:38Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a Zhang2023b</cite><br />
*[[GH95]]: fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2024</cite><br />
*[[GH150]]: λ-carrageenase Cgl150A<br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024d</cite><br />
*[[Multiple GH domain enzymes]]: mannanase Man26/5<cite>Song2024</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Zhang2024 pmid=38763726<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024 pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Shen2024d pmid=37940306<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
#Song2024 pmid=38632679<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18559User:Yaoguang Chang2024-11-04T02:32:05Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a Zhang2023b</cite><br />
*[[GH95]]: fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2024</cite><br />
*[[GH150]]: λ-carrageenase Cgl150A<br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[Multiple GH domain enzymes]]: mannanase Man26/5<cite>Song2024</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024d</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Zhang2024 pmid=38763726<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024 pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Shen2024d pmid=37940306<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
#Song2024 pmid=38632679<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18558User:Yaoguang Chang2024-11-04T02:29:11Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a Zhang2023b</cite><br />
*[[GH95]]: fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2024</cite><br />
*[[GH150]]: λ-carrageenase Cgl150A<br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[Multiple GH domain enzymes]]: mannanase Man26/5<cite>Song2024</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Zhang2024 pmid=38763726<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024 pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
#Song2024 pmid=38632679<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18557User:Yaoguang Chang2024-11-04T02:28:33Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a Zhang2023b</cite><br />
*[[GH95]]: fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2024</cite><br />
*[[GH150]]: λ-carrageenase Cgl150A<br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen 2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[Multiple GH domain enzymes]]: mannanase Man26/5<cite>Song2024</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Zhang2024 pmid=38763726<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024 pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
#Song2024 pmid=38632679<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18556User:Yaoguang Chang2024-11-04T02:26:50Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a Zhang2023b</cite><br />
*[[GH95]]: fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2024</cite><br />
*[[GH150]]: λ-carrageenase Cgl150A<br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen 2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[Multiple GH domain enzymes]]: mannanase Man26/5<cite>Song2024</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Zhang2024 pmid=37479453<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024 pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
#Song2024 pmid=38632679<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18555User:Yaoguang Chang2024-11-04T02:24:13Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a Zhang2023b</cite><br />
*[[GH95]]: α-L-fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2024</cite><br />
*[[GH150]]: λ-carrageenase Cgl150A<br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen 2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[Multiple GH domain enzymes]]: mannanase Man26/5<cite>Song2024</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Zhang2024 pmid=37479453<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024 pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
#Song2024 pmid=38632679<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18554User:Yaoguang Chang2024-11-04T02:23:36Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a Zhang2023b</cite><br />
*[[GH95]]: α-L-fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2024</cite><br />
*[[GH150]]: λ-carrageenase Cgl150A<br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen 2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[Multiple GH domain enzymes]]:mannanase Man26/5<cite>Song2024</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Zhang2024 pmid=37479453<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024 pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
#Song2024 pmid=38632679<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18553User:Yaoguang Chang2024-11-04T02:15:04Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a</cite><br />
*[[GH95]]: α-L-fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2023b</cite><br />
*[[GH150]]: λ-carrageenase Cgl150A<br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen 2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[Multiple GH domain enzymes]]:mannanase Man26/5<cite>Song2024</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024 pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
#Song2024 pmid=38632679<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18552User:Yaoguang Chang2024-11-04T02:11:24Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024a</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a</cite><br />
*[[GH95]]: α-L-fucosidase Afc95A_Wf <cite>Shen2024c</cite><br />
*[[GH96]]: α-agarase/α-funoranase BiAF96A_Aq <cite>Zhang2023b</cite><br />
*[[GH150]]: λ-carrageenase Cgl150A<br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020 Chen 2024b</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a Chen2024c</cite>, endo-1,3-fucanase Fun174Rm, endo-1,3-fucanase Fun174Ri, and endo-1,3-fucanase Fun174Sb <cite>Shen2024b</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024 pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Shen2024c pmid=38932571<br />
#Chen2024a pmid=39214858<br />
#Chen2024b pmid=38795894<br />
#Chen2024c pmid=39293626<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18551User:Yaoguang Chang2024-11-04T02:02:56Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021 Chen2024</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023a Zhang2023b</cite><br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a</cite>, endo-1,3-fucanase Fun174Rm, Fun174Ri and Fun174Sb <cite>Shen2024b</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023a pmid=36746585<br />
#Zhang2023b pmid=37479453<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024 pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Chen2024 pmid=39214858<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18550User:Yaoguang Chang2024-11-04T01:59:49Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021</cite> <cite>Chen2024</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, β-porphyranase Por16C_Wf <cite>Zhang2020</cite>, and laminarinase Lam16A_Wa<br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023</cite><br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, and endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a</cite>, endo-1,3-fucanase Fun174Rm, Fun174Ri and Fun174Sb <cite>Shen2024b</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023 pmid=36746585<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024 pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
#Chen2024 pmid=39214858<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18549User:Yaoguang Chang2024-11-04T01:50:31Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, and β-porphyranase Por16C_Wf <cite>Zhang2020</cite><br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023</cite><br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, endo-1,3-fucanase Fun168E <cite>Shen2024a</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a</cite>, endo-1,3-fucanase Fun174Rm, Fun174Ri and Fun174Sb <cite>Shen2024b</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023 pmid=36746585<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024 pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024a pmid=39389500<br />
#Shen2024b pmid=38616101<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18548User:Yaoguang Chang2024-11-04T01:47:42Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, and β-porphyranase Por16C_Wf <cite>Zhang2020</cite><br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023</cite><br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite>, endo-1,3-fucanase Fun168D <cite>Shen2023</cite>, endo-1,3-fucanase Fun168E <cite>Shen2024</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023 pmid=36746585<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024 pmid=39069041<br />
#Shen2023 pmid=37479433<br />
#Shen2024 pmid=39389500<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_106&diff=18545Carbohydrate Binding Module Family 1062024-11-01T12:55:44Z<p>Yaoguang Chang: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Wenwen Tao|Wenwen Tao]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM106.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
VbCBM106 represents the first characterized member of the CBM106 family, which is appended to a [[PL6]] potential alginate lyase found in the marine bacteria ''Vibrio breoganii''. The CBM showed the favorable specificity to alginate, while it could not bind to other polyuronic acids, such as hyaluronic acid, chondroitin sulfates, dermatan sulfate, and pectin, as well as other polysaccharides from brown algae including laminarin and fucoidan <cite>Mei2024</cite>.<br />
<br />
== Structural Features ==<br />
[[File:CBM106_Fig.1.png|thumb|350px|right|'''Figure 1. Crystal structure of VbCBM106.''' The strand, helix, and loop were colored in cyan, yellow, and white respectively. The sequential order of these strands and helices was depicted from P4 through to G200.]]<br />
The crystal structure (1.55 Å) of VbCBM106 exhibits a typical β-sandwich fold, which is composed of two antiparallel β-sheets formed by 11 β-strands and 4 helixes (Fig.1). Site-directed mutagenesis assays demonstrated that the residues R59, R61, K63, K139, and R190 play critical roles in the ligand binding of VbCBM106 <cite>Mei2024</cite>.<br />
<br />
== Functionalities == <br />
VbCBM106 and some of its homologous sequences are linked to the catalytic modules of the PL6 family or its subfamily PL6_1. In the natural environments, VbCBM106 might could enhance the catalytic efficiency of its appended enzymes by increasing the contact between adjacent catalytic domains and alginate <cite>Mei2024</cite>.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:The first member VbCBM106 is a component of a potential [[PL6]] alginate lyase from a marine bacterium ''Vibrio breoganii'' <cite>Mei2024</cite>.<br />
;First Structural Characterization<br />
:VbCBM106 ([{{PDBlink}}8zqf PDB 8zqf]) is the first and currently only member of the CBM106 family with the structural information <cite>Mei2024</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Mei2024 pmid=39069041<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM106]]<br />
<!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_96&diff=18544Carbohydrate Binding Module Family 962024-11-01T12:54:23Z<p>Yaoguang Chang: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Wenwen Tao|Wenwen Tao]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM96.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
Members of the CBM96 family are present within various CAZyme families, including [[PL8]], [[PL35]], [[GH16]], and [[GH136]], suggesting that they may possess a wide range of diverse activities. TM6-N4, originating from the marine thermophilic bacterium ''Defluviitalea phaphyphila'', and DmCBM96-1/DmCBM96-2, derived from the bacterium ''Dysgonomonas sp.'' HDW5A isolated from ''Hydrophilus acuminatus'' , are currently the characterized members of the CBM96 family. TM6-N4 is associated with the catalytic module of [[PL39]] alginate lyase, and its specific binding capability towards alginate was confirmed by affinity electrophoresis analysis. However, isothermal titration calorimetry analysis revealed that TM6-N4 exhibits no significant preference for mannuronate or guluronate oligosaccharides <cite>Ji2023</cite>. DmCBM96-1 and DmCBM96-2, which are consecutive CBMs linked to chondroitin sulfate (CS) lyase PL8_3, have been confirmed to bind to CS-A (chondroitin 4-sulfate), CS-C (chondroitin 6-sulfate), and Aj-fCS (consisting of CS-type backbone and sulfated fucose branches), but not to other polyuronic acids such as hyaluronic acid (HA), dermatan sulfate (DS), heparin (HS), pectin, and alginate. Comparatively, the relative affinity of both DmCBM96 proteins to CS-C are higher than CS-A <cite>Liu2024</cite>.<br />
<br />
== Structural Features ==<br />
[[File:CBM96_Fig.1.png|thumb|350px|right|'''Figure 1. Crystal structure of TM6-N4.''' The strand, helix, loop and Ca<Sup>2+</Sup> were colored in cyan, yellow, white and green respectively.]]<br />
Upon BLASTP analysis, DmCBM96-1 exhibits a relatively low sequence identity of approximately 32% when compared to TM6-N4, whereas the sequence identity between DmCBM96-2 and TM6-N4 is even lower, at 25%. The crystal structures of TM6-N4 (1.35 Å) and DmCBM96-1 (2.20 Å) reveal that they both exhibit a typical β-sandwich fold, comprising two antiparallel β-sheets consisting of 11 β-strands, but differ in helixes. The binding sites of both DmCBM96-1 and TM6-N4 are located within the loop regions. Site-directed mutagenesis assay revealed that the basic amino acids Arg27, Lys45, Arg53, Arg157, and the aromatic amino acid Tyr51 at the binding site of DmCBM96-1 are crucial for CS binding <cite>Liu2024</cite>. While , the amino acids located at the bottom or wall of the shallow groove of TM6-N4, including Lys10, Lys22, Lys25, Lys27, Lys31, Arg36, and Tyr159, are essential for alginate binding <cite>Ji2023</cite>. Among these, the crucial amino acids Lys45 and Arg53 in DmCBM96-1 correspond to the key amino acids Lys27 and Arg36 in TM6-N4, respectively, and they are highly conserved within the CBM96 family, suggesting their pivotal roles in the ligand binding process.<br />
<br />
== Functionalities == <br />
Members of the CBM96 family are annotated by dbCAN to be associated with several CAZyme families, and their presumed physiological role is to facilitate enzyme-carbohydrate interactions and enhance the local concentration of enzymes near substrates, thereby promoting the degradation of polysaccharides. Based on the polysaccharide-binding specificity of the CBM96 family, it may also have potential applications in the study of cellular structures or the detection of pathogenic bacteria. Furthermore, through fusion expression, CBM96 could potentially be utilized to optimize the properties of other CAZymes <cite>Ji2023</cite>.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:The TM6-N4 derived from the alginate lyase Dp0100 of marine bacterium ''Defluviitalea phaphyphila'', which was first reported in 2023, represents the first characterized member of the CBM96 family <cite>Ji2023</cite>.<br />
;First Structural Characterization<br />
:Alginate-binding protein TM6-N4 is the first member of the CBM96 family to undergo crystal structure characterization ([{{PDBlink}}7vbo PDB 7vbo]) <cite>Ji2023</cite>. Subsequently, CS-binding protein DmCBM96-1 was also characterized ([{{PDBlink}}2pqr PDB 2pqr]) <cite>Liu2024</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Ji2023 pmid=36592931<br />
#Liu2024 pmid=38805590<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM096]]<br />
<!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_70&diff=18543Carbohydrate Binding Module Family 702024-11-01T12:52:58Z<p>Yaoguang Chang: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Menghui Sun|Menghui Sun]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM70.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
The CBM70 family comprises members predominantly of bacterial origin. Notably, it is the only known family with a specific binding affinity for hyaluronic acid, a linear glycosaminoglycan composed of repeating disaccharide units of β-1,4-ᴅ-glucuronic acid-β-1,3-N-acetyl-ᴅ-glucosamine. Studies have shown that CBM70 modules typically do not bind to other glycosaminoglycans, such as chondroitin sulfate, dermatan sulfate, or heparin <cite>Michael2014 Xuanwei2022</cite>.<br />
<br />
== Structural Features ==<br />
CBM70 modules are typically composed of approximately 160 amino acids. The crystal structure of the N-terminal CBM70 module (SpCBM70) from ''S. pneumoniae'' hyaluronate lyase Hyl has been determined. SpCBM70 adopts a classic β-jelly roll fold, consisting of two opposing 5-stranded antiparallel β-sheets. This slightly bowed sandwich structure creates a groove along the concave surface, which carries a significant positive charge and is highly conserved within the CBM70 family <cite>Michael2014</cite>.[[File:CBM70.png|thumb|'''Figure 1.''' The fold of the hyaluronic acid binding molecule SpCBM70 from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl (PDB ID: 4D0Q). The structure is rotated 90 degrees to illustrate the overall fold and the arrangement of β-sheet.]]<br />
<br />
== Functionalities == <br />
CBM70 domains are commonly found as accessory modules in hyaluronate lyases produced by bacteria of the ''Streptococcus'' genus. These domains enhance the enzyme capability to degrade hyaluronic acid, a crucial component of the host's extracellular matrix. Infection by pathogens such as ''S. pneumoniae'' utilize hyaluronate lyase to break down hyaluronic acid, facilitating bacterial invasion and spread. CBM70 domains boost this process by increasing the binding efficiency of the enzyme, playing a key role in pathogen virulence and contributing to the high specificity of the enzyme for hyaluronic acid. Additionally, CBM70 domains have been effectively utilized in lateral flow immunoassays for the specific detection of hyaluronic acid, demonstrating their potential in diagnostic applications <cite>Xuanwei2022</cite>.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
The first CBM70 module to be identified (SpCBM70) was from the ''S. pneumoniae'' hyaluronate lyase Hyl.<br />
;First Structural Characterization<br />
The first crystal structure of a CBM70 module was also that of SpCBM70, PDB ID 4D0Q.<br />
<br />
== References ==<br />
<biblio><br />
#Michael2014 pmid=25100731<br />
<br />
#Xuanwei2022 pmid=36395930<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM70]]<br />
<!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_47&diff=18542Carbohydrate Binding Module Family 472024-11-01T12:51:36Z<p>Yaoguang Chang: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Wenwen Tao|Wenwen Tao]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM47.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
The C-terminal triplet fucose-binding module (SpX-1.2.3) of protein toxin SpGH98, originating from the fucose utilization operon in ''Streptococcus pneumoniae'', has been firstly designated as CBM47 <cite>Boraston2006</cite>. ''Anguilla anguilla'' agglutinin (AAA), derived from the European eel, which was characterized earlier and initially classified as an F-type lectin <cite>Bianchet2002</cite>, was also included in the CBM47 family. Several other members of CBM47 family, such as MsaFBP32 <cite>Bianchet2010</cite>, LLY<Sup>lec</Sup> <cite>Feil2012</cite> and its mutant LLY<Sup>lec</Sup>Y62H <cite>Lawrence2012</cite>, have been confirmed to possess the F-type lectin fold. The aforementioned proteins are all capable of binding to polysaccharides containing fucose, often trisaccharides or smaller, such as AAA, and a portion of CBM47 members has been demonstrated to bind to polysaccharides with galactose <cite>Bianchet2002</cite>. Both of these sugars are ubiquitous in glycoproteins and glycolipids on the cell surface, playing crucial roles in cellular bioactivity and functions. Furthermore, the CBM47 family exhibits specific binding to Lewis blood group oligosaccharides, which are characterized by fucosylation modifications. For instance, LLY<Sup>lec</Sup> binds to both Lewis y (Le<Sup>y</Sup>) antigen (type 1 antigen) and Lewis b (Le<Sup>b</Sup>) antigen (type 2 antigen) <cite>Feil2012</cite>, whereas AAA displays a preference for binding to the Le<Sup>y</Sup> antigen <cite>Bianchet2002</cite>. Consequently, the CBM47 family holds potential applications in immune recognition and disease diagnosis. Besides, a novel CBM47 domain was discovered from the marine bacterium ''Wenyingzhuangia fucanilytica'', which is appended to the GH168 family sequence. The CBM exhibited a specific binding capacity to sulfated fucans with the backbone composed of 1,3-α-L-fucopyranose residues <cite>Mei2022</cite>.<br />
<br />
== Structural Features ==<br />
[[File:CBM47_Fig.1.png|thumb|350px|right|'''Figure 1. Crystal structure of (A) AAA and (B) SpX-1.''' The strand, helix, loop, Ca<sup>2+</sup> and Cl<sup>-</sup> were colored in cyan, yellow, white ,green and origin respectively.]]<br />
The core structures of the CBM47 family exhibit remarkable similarity, adopting an eight-stranded β-sandwich fold, which is comprised of a five-stranded anti-parallel β-sheet on one side and a three-stranded anti-parallel β-sheet on the other <cite>Boraston2006 Bianchet2002 Bianchet2010 Feil2012 Lawrence2012</cite>. Additionally, CBM47 typically exists as a dimer or trimer under physiological conditions, with Ca<sup>2+</sup> playing a pivotal role in maintaining its conformational stability. The CBM47 family recognizes and binds polysaccharides through shallow grooves located within their complementarity-determining regions (CDRs), and these variable loops have been shown to exhibit a high degree of sequence and conformational variability among different CBM47s, enabling them to recognize diverse ligands. For instance, LLY<sup>lec</sup> and SpX-1 reveal smaller differences among their loops, permitting them to bind to a wide array of Lewis blood group oligosaccharides <cite>Boraston2006 Feil2012</cite>. While AAA features a particularly longer and rigid loop, which may account for its preference to form complexes with type 1 antigens while lacking affinity for type 2 antigens <cite>Bianchet2002</cite>. Polysaccharide binding via loop regions typically tends to be of shorter length. <br />
<br />
== Functionalities == <br />
The AAA, discovered in the serum of European eel, and MsaFBP32, isolated from the plasma of the striped bass ''Morone saxatilis'', participate in the recognition of bacterial lipopolysaccharides by the animal innate immune system <cite>Bianchet2002 Bianchet2010</cite>.<br />
<br />
Both LLY<sup>lec</sup> and SpX-1.2.3 are associated with bacterial toxins belonging to GH98 family. Under physiological conditions, these proteins form aggregates that bind to glycoproteins or glycolipids on the cell membrane and insert into the membrane, thereby enhancing the pore-forming activity of the toxins and accelerating cell lysis. Based on the binding specificity to fucoidan, the fluorescein isothiocyanate-labeled SpX-1.2.3 triplet was applied for in situ visualization of mouse lung tissue sections <cite>Boraston2006 Feil2012</cite>.<br />
<br />
Sulfated fucans, constituting a pivotal structural component within the body wall of sea cucumbers, are important to the overall architecture and quality of these marine invertebrates. To evaluate the feasibility of WfCBM47 as a tool in the ''in situ'' investigation of sulfated fucan, a fluorescent probe was constructed by fusing WfCBM47 with a green fluorescent protein. The ''in situ'' visualization of sulfated fucan in the sea cucumber (''Apostichopus japonicus'') body wall was implemented for the first time by utilizing the probe <cite>Mei2022</cite>.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:SpX-1.2.3, isolated from ''Streptococcus pneumoniae'' and associated with the toxin SpGH98, was reported in 2006 and was initially proposed to constitute a member of the CBM47 family <cite>Boraston2006</cite>. However, F-type lectin AAA, discovered in the serum of European eel and reported in 2002, has also been included in the CBM47 family by CAZy database <cite>Bianchet2002</cite>.<br />
;First Structural Characterization<br />
:All the fucose-binding proteins, SpX-1 ([{{PDBlink}}2j1r PDB 2j1r]), SpX-3 ([{{PDBlink}}2j22 PDB 2j22]) and AAA ([{{PDBlink}}1k12 PDB 1k12]), have had their tertiary structures determined through X-ray crystallography <cite>Boraston2006 Bianchet2002</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Boraston2006 pmid=16987809<br />
#Bianchet2002 pmid=12091873<br />
#Bianchet2010 pmid=20561530<br />
#Feil2012 pmid=22325774<br />
#Lawrence2012 pmid=23181061<br />
#Mei2022 pmid=34893209<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM047]]<br />
<!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_105&diff=18496Carbohydrate Binding Module Family 1052024-10-28T03:12:41Z<p>Yaoguang Chang: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Guanchen Liu|Guanchen Liu]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM105.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
The first member of family CBM105 (SoCBM) was identified in the [[PL29]] multidomain chondroitinase ChABC29So from ''Segatella oris'' <cite>Liu2024</cite>. SoCBM bound specifically to chondroitin sulfates (CSs) including CS-A and CS-C, while incapable of binding to other glycosaminoglycanss or polyuronic acid substrates.<br />
<br />
== Structural Features ==<br />
[[File:CBM105 Fig.1.png|thumb|350px|right|'''Figure 1. Domain analysis of ChABC29So, the parent enzyme of SoCBM.''' The enzyme consists of a signal peptide (1-21 amino acids), a PL29 domain (66-380 amino acids) and a CBM105 domain (viz., SoCBM; 555-785 amino acids).]]<br />
An AlphaFold2 model predicts that SoCBM has a β-sandwich fold (Fig.1).<br />
<br />
== Functionalities == <br />
SoCBM is the C-terminus domain of a [[PL29]] enzyme ChABC29So that displays chondroitin sulfate ABC activity, consistent with the SoCBM specificity. Biochemical characterization of ChABC29So and the CBM-truncated enzyme revealed that the SoCBM enhances the catalytic activity, thermostability, and disaccharide proportion in the final enzymatic products of ChABC29So.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
:The chondroitin sulfate binding SoCBM from the ''S. oris'' [[PL29]] chondroitinase was the first member of the family to be identified and characterized<cite>Liu2024</cite>.<br />
;First Structural Characterization<br />
:No experimentally determined three-dimensional structure has been solved in this CBM family.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2024 pmid=38777025<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM105]]<br />
<!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. --></div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=Polysaccharide_Lyase_Family_44&diff=18492Polysaccharide Lyase Family 442024-10-26T00:52:04Z<p>Yaoguang Chang: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Jinhang Zhou|Jinhang Zhou]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Polysaccharide Lyase Family PL44'''<br />
|-<br />
|'''3D Structure''' <br />
|parallel β-helix (AlphaFold)<br />
|-<br />
|'''Mechanism''' <br />
|poly-mannuronate preferred<br />
|-<br />
|'''Charge neutraliser'''<br />
|not known<br />
|-<br />
|'''Active site residues'''<br />
|not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}PL44.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Members of polysaccharide lyase family 44 have been shown to exhibit alginate lyase activity. The first member of this family is Aly44A, which originates from the bacterium ''Bacillus'' sp. FJAT-50079. (Genbank number WP_213137828.1). A total of 126 homologous sequences of Aly44A were identified by utilizing the BLASTp (with sequence coverage > 70% and identity > 40%) and CD-Hit tools. Meanwhile, four homologs of Aly44A exhibited the ability to degrade alginate <cite>Zhou2024</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
The kinetic analysis showed that Aly44A exhibited higher conversion efficiency and a stronger affinity for polyM compared to polyG, indicating Aly44A was polyM-preferred. In contrast to bifunctional alginate lyases, which exhibited no preference for polyG or polyM, Aly44A showed superior potential in the preparation of alginate oligosaccharides consisting of M-blocks. It showed that Aly44A had a higher affinity and catalytic efficiency towards the polyM region of the longer-chain alginate <cite>Zhou2024</cite>.<br />
<br />
== Action Pattern ==<br />
Based on the analysis of the action pattern, it showed that Aly44A was polyM-preferred. Aly44A was verified to exhibit a random endo-acting lyase activity to alginate. The final products of degradation were alginate oligosaccharides with DP 2-8, the main products of degradation were AOS with DP 2-4 as detected by UPSEC-MS <cite>Zhou2024</cite>.<br />
<br />
== Catalytic Residues ==<br />
No catalytic residues have been identified in this polysaccharide lyase family at present.<br />
<br />
== Three-dimensional structures ==<br />
The structure of Aly44A was predicted to be a parallel β-helix by AlphaFold2 <cite>Zhou2024</cite>.<br />
<br />
== Family Firsts ==<br />
;First description of catalytic activity<br />
The alginate lyase Aly44A was the first member of the family PL44 to be identified and characterized.<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet identified.<br />
<br />
== References ==<br />
<biblio><br />
#Zhou2024 pmid=39174099<br />
</biblio><br />
<br />
[[Category:Polysaccharide Lyase Families|PL044]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18461User:Yaoguang Chang2024-10-18T07:38:14Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, and β-porphyranase Por16C_Wf <cite>Zhang2020</cite><br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023</cite><br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite><br />
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite><br />
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024</cite><br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023 pmid=36746585<br />
#Shen2020 pmid=32849348<br />
#Liu2023a pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Liu2024a pmid=38805590<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Liu2023b pmid=37951443<br />
#Mei2023b pmid=38010608<br />
#Liu2024b pmid=38777025<br />
#Mei2024 pmid=39069041<br />
</biblio><br />
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<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18458User:Yaoguang Chang2024-10-17T07:02:43Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[PL44]], [[CBM92]], [[CBM99]] and [[CBM101]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, and β-porphyranase Por16C_Wf <cite>Zhang2020</cite><br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023</cite><br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite><br />
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite><br />
<br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023 pmid=36746585<br />
#Shen2020 pmid=32849348<br />
#Liu2023 pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
#Mei2023a pmid=37769778<br />
#Mei2023b pmid=38010608<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18457User:Yaoguang Chang2024-10-17T06:59:18Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM101]] and CBM106 families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, and β-porphyranase Por16C_Wf <cite>Zhang2020</cite><br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023</cite><br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
<br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023 pmid=36746585<br />
#Shen2020 pmid=32849348<br />
#Liu2023 pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18456User:Yaoguang Chang2024-10-17T06:58:29Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[PL44]],[[CBM92]],CBM99,CBM101 and CBM106 families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, and β-porphyranase Por16C_Wf <cite>Zhang2020</cite><br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023</cite><br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
<br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023 pmid=36746585<br />
#Shen2020 pmid=32849348<br />
#Liu2023 pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18455User:Yaoguang Chang2024-10-17T06:52:28Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[PL44]],and [[CBM92]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, and β-porphyranase Por16C_Wf <cite>Zhang2020</cite><br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023</cite><br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
<br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023 pmid=36746585<br />
#Shen2020 pmid=32849348<br />
#Liu2023 pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=18454User:Yaoguang Chang2024-10-17T06:51:25Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|100px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of [[GH168]], [[GH174]], [[PL44]],and [[CBM92]] families, and contributed to the studies related to members of the following families:<br />
<br />
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, and β-porphyranase Por16C_Wf <cite>Zhang2020</cite><br />
*[[GH29]]: fucosidase Alf1_Wf <cite>Dong2017</cite> <br />
*[[GH82]]: ι-carrageenase Cgi82A <cite>Shen2017</cite><br />
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023</cite><br />
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite><br />
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023</cite><br />
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite><br />
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite><br />
*[[CBM16]]: ABP_Wf (alginate-binding CBM) <cite>Mei2020</cite><br />
*[[CBM47]]: WfCBM47 (sulfated fucan-binding CBM) <cite>Mei2022a</cite><br />
*[[CBM70]]: SrCBM70 (hyaluronic acid-binding CBM) <cite>Mei2022b</cite><br />
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite><br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite><br />
<br />
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2020b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023 pmid=36746585<br />
#Shen2020 pmid=32849348<br />
#Liu2023 pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
#Zhou2024 pmid=39174099<br />
</biblio><br />
<br />
<br />
<br />
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<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_187&diff=17683Glycoside Hydrolase Family 1872024-01-05T06:46:10Z<p>Yaoguang Chang: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Jingjing Shen|Jingjing Shen]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH187'''<br />
|-<br />
|'''Clan''' <br />
|not known<br />
|-<br />
|'''Mechanism'''<br />
|not known<br />
|-<br />
|'''Active site residues'''<br />
|not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH187.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Members of glycoside hydrolase family 187 have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun187A from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219, specifically hydrolyzes the α-1,3-L-fucoside bonds between non-sulfated and 2-O-sulfated fucose residuess in the sulfated fucan oligosaccharide α-L-Fuc''p''(2,4OSO<sub>3</sub><sup>-</sup>)-1→3-α-L-Fuc''p''-1→3-α-L-Fuc''p''(2OSO<sub>3</sub><sup>-</sup>)-1→3-α-L-Fuc''p''(2OSO<sub>3</sub><sup>-</sup>) in an endo-acting manner <cite>Shen2024</cite>. Meanwhile, one homologue of Fun187A displays activities toward sulfated fucans from ''Holothuria tubulosa'' and ''Isostichopus badionotus'', namely WP_159020740.1 <cite>Shen2024</cite>.<br />
[[File: Figure 1.jpg|thumb|''' Figure 1. The phylogenetic tree of GH187 homologues. Sequences confirmed to exhibit α-1,3-L-fucanase activity were highlighted in red triangles.]]<br />
<br />
== Kinetics and Mechanism ==<br />
The catalytic mechanism of GH187 has not been identified. As mentioned in the report, Fun187A showed no transglycosylating activity in the tested acceptor substrates, such as D-glucose, D-galactose, D-mannose, D-fructose, L-fucose, D-glucosamine, N-acetyl-D-glucosamine, glycerin, and methanol <cite>Shen2024</cite>.<br />
<br />
== Catalytic Residues ==<br />
No catalytic residues have been identified in this glycoside hydrolase family at present.<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved in this glycoside hydrolase family at present.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet identified.<br />
<br />
== References ==<br />
<biblio><br />
#Shen2024 pmid=37940306<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycoside Hydrolase Families|GH187]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_101&diff=17682Carbohydrate Binding Module Family 1012024-01-05T06:45:01Z<p>Yaoguang Chang: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM101.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
<br />
[[File:Figure.png|thumb|'''Figure 1. Carbohydrate array assays of WfCBM101. ''' The binding of WfCBM101 to agarose and other galactans in red algae (A), and several other polysaccharides (B) was evaluated. κ-Car, κ-carrageenan. ι-Car, ι-carrageenan. Alg, alginate. An-FUC, sulfated fucan from ''Ascophyllum nodosum''. CSA, chondroitin sulfate A sodium salt. HA, hyaluronic acid. Pec, pectin. Three parallels were conducted for each polysaccharide.''' ]]<br />
<br />
The first characterized member in the CBM101 family is WfCBM101 <cite>Mei2023</cite>. The CBM WfCBM101 could bind to agarose and displayed a weak affinity to porphyran (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, WfCBM101 could bind to agarose tetrasaccharide, but not to porphyran tetrasaccharide. It was reported that the backbone of porphyran consists of approximately 30% characteristic structural units of agarose <cite>Chi2012</cite>. It was thus speculated that the weak affinity of WfCBM101 to porphyran was attributed to the structural heterogeneity of porphyran.<br />
<br />
== Structural Features ==<br />
The predicted structure by AlphaFold2 showed that WfCBM101 displays a typical β-sandwich fold. <br />
<br />
== Functionalities == <br />
To evaluate the feasibility of WfCBM101 as a tool in the ''in situ'' investigation of porphyran, a fluorescent probe was constructed by fusing WfCBM101 with a green fluorescent protein. The ''in situ'' visualization of agarose in red alga ''Gelidium amansii'' was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.<br />
Taking WfCBM101 as the query sequence, 15 modules were retrieved from the NCBI database by the BLASTP program (E-value < e<sup>-5</sup>). There are eight modules adjacent to catalytic domains which are divided into the GH16_16 subfamily or GH86 family respectively. According to the CAZy database, the GH16_16 subfamily and GH86 family members exhibit the activity for degrading agarose. It was thus implied that these eight modules might bind to agarose, which requires further investigation.<br />
<br />
== Family Firsts ==<br />
;First Identified<br />
The first member WfCBM101 is a component of a GH86 β-agarase (unpublished data) from a marine bacterium ''Wenyingzhuangia fucanilytica'' CZ1127<sup>T</sup> <cite>Chen2016</cite>.<br />
;First Structural Characterization<br />
No three-dimensional structure has been solved in this CBM family at present.<br />
<br />
== References ==<br />
<biblio><br />
#Mei2023 pmid=38010608<br />
#Chi2012 pmid=22526785<br />
#Chen2016 pmid=27220912<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM101]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_100&diff=17681Carbohydrate Binding Module Family 1002024-01-05T06:42:58Z<p>Yaoguang Chang: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Guanchen Liu|Guanchen Liu]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM100.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
[[File:Fig.1 300.png|thumb|250px|right|'''Figure 1. Domain analysis of the parent enzyme of PhCBM100.'''The enzyme consists of a signal peptide (1-23 amino acids), a PL29 domain (68-399 amino acids), a CBM100 domain (viz., PhCBM100; 555-785 amino acids) and a C-terminal sorting domain (786-851 amino acids).]]<br />
The first characterized member of the CBM100 family, PhCBM100<cite>Liu2023</cite>, was found in a PL29 putative chondroitin lyase from ''Polaribacter haliotis''. PhCBM100 bound specifically to chondroitin sulfates (CSs) including CS-A, CS-C and fucosylated chondroitin sulfate from sea cucumber ''Apostichopus japonicus'', whereas incapable of binding to other glycosaminoglycans or polyuronic acids. By affinity electrophoresis assays, PhCBM100 displays high affinity for CS-A and CS-C with the ''K''<sub>a</sub> values of 2.1×10<sup>6</sup> M<sup>-1</sup> and 6.0×10<sup>6</sup> M<sup>-1</sup>, respectively.<br />
<br />
== Structural Features ==<br />
[[File:Fig.2 300.png|thumb|400px|right|'''Figure 2. Structure of PhCBM100.''' (A) Schematic representation of PhCBM100 showing helices in yellow and strands in cyan. (B) Detailed view of the putative PhCBM100 binding site. The surface is colored by electrostatic potential, from blue (positive charge) to red (negative charge).]]<br />
The 1.55 Å resolution X-ray crystal structure of PhCBM100 ([{{PDBlink}}8jiy PDB 8jiy]) exhibited a β-sandwich fold formed by two antiparallel comprised of 10 β-strands and 2 helices.<br />
A groove with both a distinct positive charge and a high degree of conserved residues is proposed as the binding site, enriched with hydrophilic amino acids. As the result of molecular docking, the basic amino acid residues (e.g., Lys-40, Arg-122 and Arg-201) of PhCBM100 may contribute to CS binding through the ionic contacts. <br />
<br />
== Functionalities == <br />
PhCBM100 is a component of a PL29 enzyme that displays chondroitin-sulfate ABC endolyase activity, consistent with the PhCBM100 specificity. The ''in situ'' visualization of chondroitin sulfate in animal tissues (e.g., chicken cartilage, bovine muscle, and porcine laryngeal cartilage) was realized by utilizing a fluorescent probe constructed by fusing PhCBM100 with a green fluorescent protein.<br />
<br />
== Family Firsts ==<br />
;First Identified:The chondroitin sulfate binding PhCBM100 from the ''P. haliotis'' PL29 putative chondroitin lyase was the first member of the family to be identified and characterized.<br />
;First Structural Characterization:PhCBM100 was also the first structurally characterized CBM100.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2023 pmid=37951443<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM100]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=Carbohydrate_Binding_Module_Family_99&diff=17680Carbohydrate Binding Module Family 992024-01-05T06:41:56Z<p>Yaoguang Chang: </p>
<hr />
<div><br />
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Xuanwei Mei|Xuanwei Mei]]<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CBM99.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
== Ligand specificities ==<br />
<br />
[[File:Figure1.png|thumb|'''Figure 1. Carbohydrate array assay results of FvCBM99. ''' Binding analysis with porphyran and other galactans in red algae (A), and other polysaccharides (B). κ-Car, κ-carrageenan. ι-Car, ι-carrageenan. Alg, alginate. An-FUC, sulfated fucan from ''Ascophyllum nodosum''. CSA, chondroitin sulfate A sodium salt. HA, hyaluronic acid. Pec, pectin. Each polysaccharide performed three parallels. The values (noted at the bottom) were the average gray intensities of the triplicates. The value binding to porphyran was set to 100, and the other values were normalized accordingly.''' ]]<br />
<br />
The first characterized member in the CBM99 family is FvCBM99 <cite>Mei2023</cite>. The CBM FvCBM99 could bind to porphyran and displayed a weak affinity to agarose (Fig. 1). While it was incapable of binding to the other examined polysaccharides, including κ-carrageenan, ι-carrageenan, alginate, sulfated fucan, chondroitin sulfate A sodium salt, hyaluronic acid, or pectin. Furthermore, FvCBM99 could bind to porphyran tetrasaccharide with an affinity constant of 1.9 × 10<sup>-4</sup> M, but not to agarose tetrasaccharide. Since agarose chains usually contain a few characteristic structural units of porphyran <cite>Chi2012</cite>, it was thus speculated that the weak affinity of FvCBM99 to agarose was attributed to the structural heterogeneity of agarose. The polysaccharide and oligosaccharide binding assays showed that FvCBM99 specifically binds to the major structural units of porphyran.<br />
<br />
== Structural Features ==<br />
The predicted structure by AlphaFold2 showed that FvCBM99 displays a typical β-sandwich fold. <br />
<br />
== Functionalities == <br />
To evaluate the feasibility of FvCBM99 as a tool in the ''in situ'' investigation of porphyran, a fluorescent probe was constructed by fusing FvCBM99 with a green fluorescent protein. The ''in situ'' visualization of porphyran in red alga ''Porphyra haitanensis'' was realized by utilizing the fluorescent probe <cite>Mei2023</cite>.<br />
Most of the members of the CBM99 family are appended to the GH16_11, GH16_12, GH16_16, or GH16_26 subfamily, or GH86 family. As documented in the CAZy database, members of the four subfamilies and the GH86 family exhibit enzymatic activity for degrading porphyran. It suggests that multiple porphyran-binding CBMs might be present in the CBM99 family. Furthermore, the homologs of FvCBM99, including WP_102755601.1 (located from 770 to 859 amino acids) and WP_108602097.1 (located from 720 to 822 amino acids), were shown to bind to porphyran. <br />
<br />
== Family Firsts ==<br />
;First Identified<br />
The first member FvCBM99 is a component of a potential GH86 porphyranase (GenBank: AJW82063.1) from a marine bacterium ''Flammeovirga sp''. OC4 <cite>Liu2015</cite>.<br />
;First Structural Characterization<br />
No three-dimensional structure has been solved in this CBM family at present.<br />
<br />
== References ==<br />
<biblio><br />
#Mei2023 pmid=37769778<br />
#Chi2012 pmid=22526785<br />
#Liu2015 pmid=25683442<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Carbohydrate Binding Module Families|CBM099]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_174&diff=17267Glycoside Hydrolase Family 1742023-05-26T08:48:46Z<p>Yaoguang Chang: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: [[User:Guanchen Liu|Guanchen Liu]]<br />
<br />
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]<br />
<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH174'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH174.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Members of [[GH174|glycoside hydrolase family 174]] have been shown to exhibit α-1,3-L-fucanase activity. The first member of this family, Fun174A from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219, specifically hydrolyze the α-1,3- L-fucoside bonds between 2-O-sulfated and non-sulfated fucose residues in the sulfated fucan from sea cucumber ''Isostichopus badionotus'' in a processive endo-acting manner.<cite>Liu2023</cite> Meanwhile, three homologs of Fun174A from ''Rubritalea marina'', ''Spartobacteria bacterium'' and ''Wenyingzhuangia fucanilytica'', display activities toward sulfated fucan from ''Isostichopus badionotus''.<cite>Liu2023</cite> All 92 members (up to May,2023) of GH174 are bacterial enzymes.<br />
[[File:Tree.png|thumb|'''Figure 1. The phylogenetic tree of GH174 homologs.''' Sequences comfirmed to exhibit α-1,3-L-fucanase activity were in red.]]<br />
<br />
== Kinetics and Mechanism ==<br />
The catalytic mechanism of GH174 has not been identified. As mentioned in the report, Fun174A showed no transglycosylating activity in the tested acceptor substrates, such as glycerin, methanol, L-fucose, D-glucose, D-galactose, D-fructose, D-mannose, D-glucosamine and N-acetyl- D-glucosamine.<cite>Liu2023</cite><br />
<br />
== Catalytic Residues ==<br />
Multiple sequence alignments of GH174 homologs showed that D119, E120 and E218 in Fun174A were highly conserved in all sequences. Three single-site mutants D119E, E120A and E218Q were established, expressed and identified in the report. Mutant D119E, E120A and E218Q resulted in 100.0%, 85.7% and 88.3% loss of activity on sulfated fucan from ''Isostichopus badionotus'' respectively. It indicated that D119, E120 and E218 were critical for the functioning of Fun174A.<cite>Liu2023</cite><br />
[[File:Weblogo.jpg|thumb|'''Figure 2. Multiple sequence alignments of residues in GH174 homologs.''' The highly conserved acidic amino acids in all sequences were indicated with black triangles.]]<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved in this glycoside hydrolase family at present. <br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Not yet identified.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet identified.<br />
<br />
== References ==<br />
<biblio><br />
#Liu2023 pmid=36746582<br />
</biblio><br />
<br />
<!-- Do not delete this Category tag --><br />
[[Category:Glycoside Hydrolase Families|GH174]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=17236User:Yaoguang Chang2023-04-20T03:14:17Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|thumb]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of CAZymes and carbohydrate-binding modules for marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of GH168, GH174, and CBM92 families, and contributed to the studies related to members of the following families:<br />
<br />
*GH16: κ-carrageenase Cgk16A [1], βκ-carrageenase Cgbk16A_Wf [2], β-porphyranase Por16A_Wf [3], and β-porphyranase Por16C_Wf [4]<br />
*GH29: fucosidase Alf1_Wf [5] <br />
*GH82: ι-carrageenase Cgi82A [6]<br />
*GH86: β-agarase Aga86A_Wa [7-8]<br />
*GH168: endo-1,3-fucanase Fun168A [9]<br />
*GH174: endo-1,3-fucanase Fun174A [10]<br />
*PL7: alginate lyase Aly7B_Wf [11]<br />
*CBM16: ABP_Wf (alginate-binding CBM) [12] <br />
*CBM47: WfCBM47 (sulfated fucan-binding CBM) [13]<br />
*CBM70: SrCBM70 (hyaluronic acid-binding CBM) [14]<br />
*CBM92: Cgk16A-CBM92 (carrageenan-binding CBM) [15]<br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) [16]<br />
<br />
Some of the above biotechnological tools have been successfully integrated with glycomics [17-18], lateral flow immunoassay [14], and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities [19-20].<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023 pmid=36746585<br />
#Shen2020 pmid=32849348<br />
#Liu2023 pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=17235User:Yaoguang Chang2023-04-20T02:28:09Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|thumb]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of CAZymes and carbohydrate-binding modules for marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of GH168, GH174, and CBM92 families, and contributed to the studies related to members of the following families:<br />
<br />
*GH16: κ-carrageenase Cgk16A [1], βκ-carrageenase Cgbk16A_Wf [2], β-porphyranase Por16A_Wf [3], and β-porphyranase Por16C_Wf [4]<br />
*GH29: fucosidase Alf1_Wf [5] <br />
*GH82: ι-carrageenase Cgi82A [6]<br />
*GH86: β-agarase Aga86A_Wa [7-8]<br />
*GH168: endo-1,3-fucanase Fun168A [9]<br />
*GH174: endo-1,3-fucanase Fun174A [10]<br />
*PL7: alginate lyase Aly7B_Wf [11]<br />
*CBM16: ABP_Wf (alginate-binding CBM) [12] <br />
*CBM47: WfCBM47 (sulfated fucan-binding CBM) [13]<br />
*CBM70: SrCBM70 (hyaluronic acid-binding CBM) [14]<br />
*CBM92: Cgk16A-CBM92 (carrageenan-binding CBM; the first member of the CBM92 family) [15]<br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) [16]<br />
<br />
Some of the above biotechnological tools have been successfully integrated with glycomics [17-18], lateral flow immunoassay [14], and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities [19-20].<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023 pmid=36746585<br />
#Shen2020 pmid=32849348<br />
#Liu2023 pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=17234User:Yaoguang Chang2023-04-20T02:22:24Z<p>Yaoguang Chang: </p>
<hr />
<div>[[File:Yaoguang Chang.jpg|thumb]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of CAZymes and carbohydrate-binding modules for marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of GH168, GH174, and CBM92 families, and contributed to the studies related to members of the following families:<br />
<br />
*GH16: κ-carrageenase Cgk16A [1], βκ-carrageenase Cgbk16A_Wf [2], β-porphyranase Por16A_Wf [3], and β-porphyranase Por16C_Wf [4]<br />
*GH29: fucosidase Alf1_Wf [5] <br />
*GH82: ι-carrageenase Cgi82A [6]<br />
*GH86: β-agarase Aga86A_Wa [7-8]<br />
*GH168: endo-1,3-fucanase Fun168A [9]<br />
*GH174: endo-1,3-fucanase Fun174A [10]<br />
*PL7: alginate lyase Aly7B_Wf [11]<br />
*CBM16: ABP_Wf (alginate-binding CBM)[12] <br />
*CBM47: WfCBM47 (sulfated fucan-binding CBM) [13]<br />
*CBM70: SrCBM70 (hyaluronic acid-binding CBM) [14]<br />
*CBM92: Cgk16A-CBM92 (carrageenan-binding CBM; the first member of the CBM92 family) [15]<br />
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) [16]<br />
<br />
Some of the above biotechnological tools have been successfully integrated with glycomics [17-18], lateral flow immunoassay [14], and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities [19-20].<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023 pmid=36746585<br />
#Shen2020 pmid=32849348<br />
#Liu2023 pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=File:Yaoguang_Chang.jpg&diff=17226File:Yaoguang Chang.jpg2023-04-20T00:33:09Z<p>Yaoguang Chang: Yaoguang Chang uploaded a new version of File:Yaoguang Chang.jpg</p>
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<div>Yaoguang Chang</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=File:Yaoguang_Chang.jpg&diff=17225File:Yaoguang Chang.jpg2023-04-20T00:31:35Z<p>Yaoguang Chang: Yaoguang Chang uploaded a new version of File:Yaoguang Chang.jpg</p>
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<div>Yaoguang Chang</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=17224User:Yaoguang Chang2023-04-20T00:19:39Z<p>Yaoguang Chang: </p>
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<div>[[File:Yaoguang Chang.jpg|thumb]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of CAZymes and carbohydrate-binding modules for marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of GH168, GH174, and CBM92 families, and contributed to the studies related to members of the following families:<br />
<br />
*GH16: κ-carrageenase Cgk16A [1], βκ-carrageenase Cgbk16A_Wf [2], β-porphyranase Por16A_Wf [3], and β-porphyranase Por16C_Wf [4]<br />
*GH29: fucosidase Alf1_Wf [5] <br />
*GH82: ι-carrageenase Cgi82A [6]<br />
*GH86: β-agarase Aga86A_Wa [7-8]<br />
*GH168: endo-1,3-fucanase Fun168A [9]<br />
*GH174: endo-1,3-fucanase Fun174A [10]<br />
*PL7: alginate lyase Aly7B_Wf [11]<br />
*CBM16: alginate-binding CBM [12] <br />
*CBM47: sulfated fucan-binding CBM WfCBM47 [13]<br />
*CBM70: hyaluronic acid-binding CBM SrCBM70 [14]<br />
*CBM92: carrageenan-binding CBM Cgk16A-CBM92 [15]<br />
*CBMnc: sulfated fucan-binding CBM Fun174A-CBM [16]<br />
<br />
Some of the above biotechnological tools have been successfully integrated with glycomics [17-18], lateral flow immunoassay [14], and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities [19-20].<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023 pmid=36746585<br />
#Shen2020 pmid=32849348<br />
#Liu2023 pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
</biblio><br />
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[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=File:Yaoguang_Chang.jpg&diff=17223File:Yaoguang Chang.jpg2023-04-20T00:19:14Z<p>Yaoguang Chang: </p>
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<div>Yaoguang Chang</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=17222User:Yaoguang Chang2023-04-20T00:16:25Z<p>Yaoguang Chang: </p>
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<div>[[Image:Blank_user-200px.png|200px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of CAZymes and carbohydrate-binding modules for marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of GH168, GH174, and CBM92 families, and contributed to the studies related to members of the following families:<br />
<br />
*GH16: κ-carrageenase Cgk16A [1], βκ-carrageenase Cgbk16A_Wf [2], β-porphyranase Por16A_Wf [3], and β-porphyranase Por16C_Wf [4]<br />
*GH29: fucosidase Alf1_Wf [5] <br />
*GH82: ι-carrageenase Cgi82A [6]<br />
*GH86: β-agarase Aga86A_Wa [7-8]<br />
*GH168: endo-1,3-fucanase Fun168A [9]<br />
*GH174: endo-1,3-fucanase Fun174A [10]<br />
*PL7: alginate lyase Aly7B_Wf [11]<br />
*CBM16: alginate-binding CBM [12] <br />
*CBM47: sulfated fucan-binding CBM WfCBM47 [13]<br />
*CBM70: hyaluronic acid-binding CBM SrCBM70 [14]<br />
*CBM92: carrageenan-binding CBM Cgk16A-CBM92 [15]<br />
*CBMnc: sulfated fucan-binding CBM Fun174A-CBM [16]<br />
<br />
Some of the above biotechnological tools have been successfully integrated with glycomics [17-18], lateral flow immunoassay [14], and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities [19-20].<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023 pmid=36746585<br />
#Shen2020 pmid=32849348<br />
#Liu2023 pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
</biblio><br />
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<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=17221User:Yaoguang Chang2023-04-20T00:16:04Z<p>Yaoguang Chang: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of CAZymes and carbohydrate-binding modules for marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of GH168, GH174, and CBM92 families, and contributed to the studies related to members of the following families:<br />
<br />
*GH16: κ-carrageenase Cgk16A [1], βκ-carrageenase Cgbk16A_Wf [2], β-porphyranase Por16A_Wf [3], and β-porphyranase Por16C_Wf [4]<br />
*GH29: fucosidase Alf1_Wf [5] <br />
*GH82: ι-carrageenase Cgi82A [6]<br />
GH86: β-agarase Aga86A_Wa [7-8]<br />
GH168: endo-1,3-fucanase Fun168A [9]<br />
GH174: endo-1,3-fucanase Fun174A [10]<br />
PL7: alginate lyase Aly7B_Wf [11]<br />
CBM16: alginate-binding CBM [12] <br />
CBM47: sulfated fucan-binding CBM WfCBM47 [13]<br />
CBM70: hyaluronic acid-binding CBM SrCBM70 [14]<br />
CBM92: carrageenan-binding CBM Cgk16A-CBM92 [15]<br />
CBMnc: sulfated fucan-binding CBM Fun174A-CBM [16]<br />
<br />
Some of the above biotechnological tools have been successfully integrated with glycomics [17-18], lateral flow immunoassay [14], and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities [19-20].<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023 pmid=36746585<br />
#Shen2020 pmid=32849348<br />
#Liu2023 pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
</biblio><br />
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<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=17220User:Yaoguang Chang2023-04-20T00:15:09Z<p>Yaoguang Chang: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of CAZymes and carbohydrate-binding modules for marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of GH168, GH174, and CBM92 families, and contributed to the studies related to members of the following families:<br />
<br />
GH16: κ-carrageenase Cgk16A [1], βκ-carrageenase Cgbk16A_Wf [2], β-porphyranase Por16A_Wf [3], and β-porphyranase Por16C_Wf [4]<br />
GH29: fucosidase Alf1_Wf [5] <br />
GH82: ι-carrageenase Cgi82A [6]<br />
GH86: β-agarase Aga86A_Wa [7-8]<br />
GH168: endo-1,3-fucanase Fun168A [9]<br />
GH174: endo-1,3-fucanase Fun174A [10]<br />
PL7: alginate lyase Aly7B_Wf [11]<br />
CBM16: alginate-binding CBM [12] <br />
CBM47: sulfated fucan-binding CBM WfCBM47 [13]<br />
CBM70: hyaluronic acid-binding CBM SrCBM70 [14]<br />
CBM92: carrageenan-binding CBM Cgk16A-CBM92 [15]<br />
CBMnc: sulfated fucan-binding CBM Fun174A-CBM [16]<br />
<br />
Some of the above biotechnological tools have been successfully integrated with glycomics [17-18], lateral flow immunoassay [14], and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities [19-20].<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023 pmid=36746585<br />
#Shen2020 pmid=32849348<br />
#Liu2023 pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022a pmid=34893209<br />
#Mei2022b pmid=36395930<br />
#Mei2022c pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Changhttps://www.cazypedia.org/index.php?title=User:Yaoguang_Chang&diff=17219User:Yaoguang Chang2023-04-20T00:13:22Z<p>Yaoguang Chang: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of CAZymes and carbohydrate-binding modules for marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. <br />
His research group discovered the first member of GH168, GH174, and CBM92 families, and contributed to the studies related to members of the following families:<br />
<br />
GH16: κ-carrageenase Cgk16A [1], βκ-carrageenase Cgbk16A_Wf [2], β-porphyranase Por16A_Wf [3], and β-porphyranase Por16C_Wf [4]<br />
GH29: fucosidase Alf1_Wf [5] <br />
GH82: ι-carrageenase Cgi82A [6]<br />
GH86: β-agarase Aga86A_Wa [7-8]<br />
GH168: endo-1,3-fucanase Fun168A [9]<br />
GH174: endo-1,3-fucanase Fun174A [10]<br />
PL7: alginate lyase Aly7B_Wf [11]<br />
CBM16: alginate-binding CBM [12] <br />
CBM47: sulfated fucan-binding CBM WfCBM47 [13]<br />
CBM70: hyaluronic acid-binding CBM SrCBM70 [14]<br />
CBM92: carrageenan-binding CBM Cgk16A-CBM92 [15]<br />
CBMnc: sulfated fucan-binding CBM Fun174A-CBM [16]<br />
<br />
Some of the above biotechnological tools have been successfully integrated with glycomics [17-18], lateral flow immunoassay [14], and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities [19-20].<br />
<br />
== References ==<br />
<biblio><br />
#Shen2018 pmid=29355636<br />
#Cao2021 pmid=34421852<br />
#Zhang2019 pmid=31352784<br />
#Zhang2020 pmid=32520542<br />
#Dong2017 pmid=27576198<br />
#Shen2017 pmid=28760444<br />
#Cao2020 pmid=32578425<br />
#Zhang2023 pmid=36746585<br />
#Shen2020 pmid=32849348<br />
#Liu2023 pmid=36746582<br />
#Pei2019 pmid=30248453<br />
#Mei2020 pmid=32747278<br />
#Mei2022 pmid=34893209<br />
#Mei2022 pmid=36395930<br />
#Mei2022 pmid=35830544<br />
#Mei2023 pmid=36924869<br />
#Chen2021 pmid=34420739<br />
#Chen2023 pmid=37059545<br />
#Cheng2022 pmid=35667104<br />
#Li2021 pmid=34415766<br />
</biblio><br />
<br />
<br />
<br />
<br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Chang,Yaoguang]]</div>Yaoguang Chang