User:Vincent Eijsink

Vincent Eijsink obtained an MSc in Molecular Sciences (Biochemistry) from Wageningen University and completed his PhD at the Groningen Biomolecular Sciences and Biotechnology Institute under the supervision of Gerard Venema in 1991. During his Ph.D. studies, focusing on the engineering of protein stability, he was co-supervised by Herman Berendsen, Bauke Dijkstra and Gert Vriend and he had several short stays in the Bioinformatics group at EMBL. In 1993, he moved to what is now called the Norwegian University of Life Sciences (NMBU), in Ås, Norway, where he became a full professor of Biochemistry in 1997. Work on CAZymes started off with work on family 18 chitinases in the late 1990s, resulting in several papers on the structure and function of these enzymes [1, 2]. Current chitin-related work focuses on family 18 chitinases [3, 4, 5] and family 19 chitinases [6], whereas the group has a growing interest and activity in chitin deacetylases (CE family 4) [7, 8]. Recent research includes CAZyme discovery [9, 10, 11]. The Eijsink group is probably best known for the discovery of lytic polysaccharide monooxygenases (LPMOs) in 2010 [12] after originally having detected chitinase boosting activity of what we now know is a chitin-active family 10 LPMO in 2005 [13]. The group demonstrated AA10 activity on cellulose [14, 15] and was the first to describe LPMO activity on soluble substrates [16, 17, 18, 19, 20, 21]. Recent developments include studies of substrate-binding [22], LPMO activation [23], and the involvement of hydrogen peroxide in LPMO action [24, 25].

References

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2. van Aalten DM, Komander D, Synstad B, Gåseidnes S, Peter MG, and Eijsink VG. (2001). Structural insights into the catalytic mechanism of a family 18 exo-chitinase. Proc Natl Acad Sci U S A. 2001;98(16):8979-84. DOI:10.1073/pnas.151103798 |
3. Horn SJ, Sikorski P, Cederkvist JB, Vaaje-Kolstad G, Sørlie M, Synstad B, Vriend G, Vårum KM, and Eijsink VG. (2006). Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides. Proc Natl Acad Sci U S A. 2006;103(48):18089-94. DOI:10.1073/pnas.0608909103 |
4. Zakariassen H, Aam BB, Horn SJ, Vårum KM, Sørlie M, and Eijsink VG. (2009). Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency. J Biol Chem. 2009;284(16):10610-7. DOI:10.1074/jbc.M900092200 |
6. Hoell IA, Dalhus B, Heggset EB, Aspmo SI, and Eijsink VG. (2006). Crystal structure and enzymatic properties of a bacterial family 19 chitinase reveal differences from plant enzymes. FEBS J. 2006;273(21):4889-900. DOI:10.1111/j.1742-4658.2006.05487.x |
10. 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 |
16. Isaksen T, Westereng B, Aachmann FL, Agger JW, Kracher D, Kittl R, Ludwig R, Haltrich D, Eijsink VG, and Horn SJ. (2014). A C4-oxidizing lytic polysaccharide monooxygenase cleaving both cellulose and cello-oligosaccharides. J Biol Chem. 2014;289(5):2632-42. DOI:10.1074/jbc.M113.530196 |