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User:Henrik Stalbrand

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Henrik Stalbrand is professor in Biochemistry at Lund University. His research group is focusing on the structure, function and applications of carbohydrate active enzymes, in particular hemicellulases [1, 2]. He obtained his PhD at Lund University in 1995 supervised by Folke Tjerneld. During a period he was visiting reseacher at VTT Biotechnology (Espoo) and during 1995 to 1997 he was a post doctoral fellow at UBC (Vancouver) with professor R.A.J. Warren and colleagues. He then joined Lund university and established his research group. Henrik´s research includes beta-mannanases (e.g. GH5 [3, 4] and GH26) [5, 6, 7] , alpha-galactosidases (e.g. GH27 and GH36) [8], and related enzymes [9].

  1. Gilbert HJ, Stålbrand H, and Brumer H. (2008). How the walls come crumbling down: recent structural biochemistry of plant polysaccharide degradation. Curr Opin Plant Biol. 2008;11(3):338-48. DOI:10.1016/j.pbi.2008.03.004 | PubMed ID:18430603 [Gilbert2008]
  2. Coutinho PM, Andersen MR, Kolenova K, vanKuyk PA, Benoit I, Gruben BS, Trejo-Aguilar B, Visser H, van Solingen P, Pakula T, Seiboth B, Battaglia E, Aguilar-Osorio G, de Jong JF, Ohm RA, Aguilar M, Henrissat B, Nielsen J, Stålbrand H, and de Vries RP. (2009). Post-genomic insights into the plant polysaccharide degradation potential of Aspergillus nidulans and comparison to Aspergillus niger and Aspergillus oryzae. Fungal Genet Biol. 2009;46 Suppl 1:S161-S169. DOI:10.1016/j.fgb.2008.07.020 | PubMed ID:19618505 [Coutinho2009]
  3. Couturier M, Roussel A, Rosengren A, Leone P, Stålbrand H, and Berrin JG. (2013). Structural and biochemical analyses of glycoside hydrolase families 5 and 26 β-(1,4)-mannanases from Podospora anserina reveal differences upon manno-oligosaccharide catalysis. J Biol Chem. 2013;288(20):14624-14635. DOI:10.1074/jbc.M113.459438 | PubMed ID:23558681 [Couturier2013]
  4. Larsson AM, Anderson L, Xu B, Muñoz IG, Usón I, Janson JC, Stålbrand H, and Ståhlberg J. (2006). Three-dimensional crystal structure and enzymic characterization of beta-mannanase Man5A from blue mussel Mytilus edulis. J Mol Biol. 2006;357(5):1500-10. DOI:10.1016/j.jmb.2006.01.044 | PubMed ID:16487541 [Larsson2006]
  5. Bågenholm V, Reddy SK, Bouraoui H, Morrill J, Kulcinskaja E, Bahr CM, Aurelius O, Rogers T, Xiao Y, Logan DT, Martens EC, Koropatkin NM, and Stålbrand H. (2017). Galactomannan Catabolism Conferred by a Polysaccharide Utilization Locus of Bacteroides ovatus: ENZYME SYNERGY AND CRYSTAL STRUCTURE OF A β-MANNANASE. J Biol Chem. 2017;292(1):229-243. DOI:10.1074/jbc.M116.746438 | PubMed ID:27872187 [Bagenholm2017]
  6. Hekmat O, Lo Leggio L, Rosengren A, Kamarauskaite J, Kolenova K, and Stålbrand H. (2010). Rational engineering of mannosyl binding in the distal glycone subsites of Cellulomonas fimi endo-beta-1,4-mannanase: mannosyl binding promoted at subsite -2 and demoted at subsite -3. Biochemistry. 2010;49(23):4884-96. DOI:10.1021/bi100097f | PubMed ID:20426480 [Hekmat2010]
  7. Le Nours J, Anderson L, Stoll D, Stålbrand H, and Lo Leggio L. (2005). The structure and characterization of a modular endo-beta-1,4-mannanase from Cellulomonas fimi. Biochemistry. 2005;44(38):12700-8. DOI:10.1021/bi050779v | PubMed ID:16171384 [Lenours2005]
  8. Reddy SK, Bågenholm V, Pudlo NA, Bouraoui H, Koropatkin NM, Martens EC, and Stålbrand H. (2016). A β-mannan utilization locus in Bacteroides ovatus involves a GH36 α-galactosidase active on galactomannans. FEBS Lett. 2016;590(14):2106-18. DOI:10.1002/1873-3468.12250 | PubMed ID:27288925 [Reddy2016]
  9. Reddy SK, Rosengren A, Klaubauf S, Kulkarni T, Karlsson EN, de Vries RP, and Stålbrand H. (2013). Phylogenetic analysis and substrate specificity of GH2 β-mannosidases from Aspergillus species. FEBS Lett. 2013;587(21):3444-9. DOI:10.1016/j.febslet.2013.08.029 | PubMed ID:24021641 [Reddy2013]

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