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User:Johan Larsbrink
Associate Professor at the Department of Life Sciences, Chalmers University of Technology.
Background
I obtained a MSc degree in Biotechnology at the Royal Institute of Technology (KTH) in 2007, where I later also completed my PhD thesis under the supervision of Harry Brumer, focusing on xyloglucan degradation [1, 2, 3]. After my PhD I worked as a postdoctoral fellow with Phil Pope and Vincent Eijsink at the Norwegian University of Life Sciences (NMBU), mainly on chitin degradation [4]. In 2015 I was appointed Assistant Professor at Chalmers University of Technology, and in 2019 I was promoted to Associate Professor. My research focuses primarily on enzyme (CAZyme) discovery coupled to structural and biochemical characterization.
I have contributed to structure-function studies of CAZymes from various families, including GH5 [2], GH18 [5], GH31 [1, 2, 6], GH35 [3], and CE15 [7, 8, 9, 10, 11].
Selected papers
- Larsbrink J, Izumi A, Ibatullin FM, Nakhai A, Gilbert HJ, Davies GJ, and Brumer H. (2011). Structural and enzymatic characterization of a glycoside hydrolase family 31 α-xylosidase from Cellvibrio japonicus involved in xyloglucan saccharification. Biochem J. 2011;436(3):567-80. DOI:10.1042/BJ20110299 |
- Larsbrink J, Rogers TE, Hemsworth GR, McKee LS, Tauzin AS, Spadiut O, Klinter S, Pudlo NA, Urs K, Koropatkin NM, Creagh AL, Haynes CA, Kelly AG, Cederholm SN, Davies GJ, Martens EC, and Brumer H. (2014). A discrete genetic locus confers xyloglucan metabolism in select human gut Bacteroidetes. Nature. 2014;506(7489):498-502. DOI:10.1038/nature12907 |
- Larsbrink J, Thompson AJ, Lundqvist M, Gardner JG, Davies GJ, and Brumer H. (2014). A complex gene locus enables xyloglucan utilization in the model saprophyte Cellvibrio japonicus. Mol Microbiol. 2014;94(2):418-33. DOI:10.1111/mmi.12776 |
- Larsbrink J, Zhu Y, Kharade SS, Kwiatkowski KJ, Eijsink VG, Koropatkin NM, McBride MJ, and Pope PB. (2016). A polysaccharide utilization locus from Flavobacterium johnsoniae enables conversion of recalcitrant chitin. Biotechnol Biofuels. 2016;9:260. DOI:10.1186/s13068-016-0674-z |
- Mazurkewich S, Helland R, Mackenzie A, Eijsink VGH, Pope PB, Brändén G, and Larsbrink J. (2020). Structural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae. Sci Rep. 2020;10(1):13775. DOI:10.1038/s41598-020-70749-w |
- Larsbrink J, Izumi A, Hemsworth GR, Davies GJ, and Brumer H. (2012). Structural enzymology of Cellvibrio japonicus Agd31B protein reveals α-transglucosylase activity in glycoside hydrolase family 31. J Biol Chem. 2012;287(52):43288-99. DOI:10.1074/jbc.M112.416511 |
- 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 |
- Arnling Bååth J, Mazurkewich S, Poulsen JN, Olsson L, Lo Leggio L, and Larsbrink J. (2019). Structure-function analyses reveal that a glucuronoyl esterase from Teredinibacter turnerae interacts with carbohydrates and aromatic compounds. J Biol Chem. 2019;294(16):6635-6644. DOI:10.1074/jbc.RA119.007831 |
- Mazurkewich S, Poulsen JN, Lo Leggio L, and Larsbrink J. (2019). Structural and biochemical studies of the glucuronoyl esterase OtCE15A illuminate its interaction with lignocellulosic components. J Biol Chem. 2019;294(52):19978-19987. DOI:10.1074/jbc.RA119.011435 |
- Krska D, Mazurkewich S, Brown HA, Theibich Y, Poulsen JN, Morris AL, Koropatkin NM, Lo Leggio L, and Larsbrink J. (2021). Structural and Functional Analysis of a Multimodular Hyperthermostable Xylanase-Glucuronoyl Esterase from Caldicellulosiruptor kristjansonii. Biochemistry. 2021;60(27):2206-2220. DOI:10.1021/acs.biochem.1c00305 |
- Zong Z, Mazurkewich S, Pereira CS, Fu H, Cai W, Shao X, Skaf MS, Larsbrink J, and Lo Leggio L. (2022). Mechanism and biomass association of glucuronoyl esterase: an α/β hydrolase with potential in biomass conversion. Nat Commun. 2022;13(1):1449. DOI:10.1038/s41467-022-28938-w |