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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
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- 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 |
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- 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 |
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- 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 |
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- 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 |