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Difference between revisions of "User:Jenny Arnling Bååth"

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PhD student at the Department of Biology and Biological engineering, [http://www.chalmers.se Chalmers University of Technology].
  
Jenny Arnling Bååth holds a master's degree in biotechnology from Lund University. She is currently a PhD student at the division of industrial biotechnology at Chalmers University of Technology.
 
  
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== Background ==
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I hold a MSc in Biotechnology from Lund University, which involved a year at Vienna University of Technology and work on the lactose metabolism in ''T. reesei'' <cite>Ivanova2013</cite>. In 2014, I started my PhD studies at Chalmers University of Technology under supervision of Prof. Lisbeth Olsson and Asst. Prof. [[User:Johan Larsbrink|Johan Larsbrink]]. I am currently finalising my PhD thesis and will graduate in February 2019. My research concerns the controlled deconstruction of plant biomass <cite>ArnlingBaath2018b</cite>, in particular glucuronoyl esterases <cite>ArnlingBaath2016, ArnlingBaath2018a</cite> belonging to [[Carbohydrate Esterase Family 15]].  
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I have been involved in structure-function studies of bacterial [[CE15]] enzymes <cite>ArnlingBaath2018a</cite>, where my main contribution has been biochemical characterisation of [[CE15]] enzymes on model substrates and native lignin-carbohydrate ester bonds.
  
  
  
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== Selected papers ==
  
 
<biblio>
 
<biblio>
#Arnling-Bååth2018 pmid=30083226
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#ArnlingBaath2018a pmid=30083226
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#ArnlingBaath2018b pmid=29713374
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#Lee2018 pmid=29110486
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#ArnlingBaath2016 pmid=27397104
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#Ivanova2013 pmid=23690947
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Latest revision as of 14:34, 18 December 2021

Jenny arnling bååth.jpg

PhD student at the Department of Biology and Biological engineering, Chalmers University of Technology.


Background

I hold a MSc in Biotechnology from Lund University, which involved a year at Vienna University of Technology and work on the lactose metabolism in T. reesei [1]. In 2014, I started my PhD studies at Chalmers University of Technology under supervision of Prof. Lisbeth Olsson and Asst. Prof. Johan Larsbrink. I am currently finalising my PhD thesis and will graduate in February 2019. My research concerns the controlled deconstruction of plant biomass [2], in particular glucuronoyl esterases [3, 4] belonging to Carbohydrate Esterase Family 15.

I have been involved in structure-function studies of bacterial CE15 enzymes [4], where my main contribution has been biochemical characterisation of CE15 enzymes on model substrates and native lignin-carbohydrate ester bonds.


Selected papers

  1. Ivanova C, Bååth JA, Seiboth B, and Kubicek CP. (2013). Systems analysis of lactose metabolism in Trichoderma reesei identifies a lactose permease that is essential for cellulase induction. PLoS One. 2013;8(5):e62631. DOI:10.1371/journal.pone.0062631 | PubMed ID:23690947 [Ivanova2013]
  2. Arnling Bååth J, Martínez-Abad A, Berglund J, Larsbrink J, Vilaplana F, and Olsson L. (2018). Mannanase hydrolysis of spruce galactoglucomannan focusing on the influence of acetylation on enzymatic mannan degradation. Biotechnol Biofuels. 2018;11:114. DOI:10.1186/s13068-018-1115-y | PubMed ID:29713374 [ArnlingBaath2018b]
  3. Arnling Bååth J, Giummarella N, Klaubauf S, Lawoko M, and Olsson L. (2016). A glucuronoyl esterase from Acremonium alcalophilum cleaves native lignin-carbohydrate ester bonds. FEBS Lett. 2016;590(16):2611-8. DOI:10.1002/1873-3468.12290 | PubMed ID:27397104 [ArnlingBaath2016]
  4. Arnling Bååth J, Mazurkewich S, Knudsen RM, Poulsen JN, Olsson L, Lo Leggio L, and Larsbrink J. (2018). Biochemical and structural features of diverse bacterial glucuronoyl esterases facilitating recalcitrant biomass conversion. Biotechnol Biofuels. 2018;11:213. DOI:10.1186/s13068-018-1213-x | PubMed ID:30083226 [ArnlingBaath2018a]
  5. Lee YC, Bååth JA, Bastle RM, Bhattacharjee S, Cantoria MJ, Dornan M, Gamero-Estevez E, Ford L, Halova L, Kernan J, Kürten C, Li S, Martinez J, Sachan N, Sarr M, Shan X, Subramanian N, Rivera K, Pappin D, and Lin SH. (2018). Impact of Detergents on Membrane Protein Complex Isolation. J Proteome Res. 2018;17(1):348-358. DOI:10.1021/acs.jproteome.7b00599 | PubMed ID:29110486 [Lee2018]

All Medline abstracts: PubMed