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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, 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 work focuses on family 18 chitinases [3, 4, 5] and family 19 chitinases [6, 7], whereas the group has a growing interest and activity in the area of chitin deacetylases (CE family 4) and cellulases [8]. Another research focus concerns proteins belonging to CBM family 33 that facilitate degradation of crystalline polymeric substrates such as chitin by glycoside hydrolases [9, 10, 11].

References

1. van Aalten DM, Synstad B, Brurberg MB, Hough E, Riise BW, Eijsink VG, and Wierenga RK. Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-A resolution. Proc Natl Acad Sci U S A 2000 May 23; 97(11) 5842-7. pmid:10823940. PubMed HubMed [VanAalten2000]
2. van Aalten DM, Komander D, Synstad B, Gåseidnes S, Peter MG, and Eijsink VG. Structural insights into the catalytic mechanism of a family 18 exo-chitinase. Proc Natl Acad Sci U S A 2001 Jul 31; 98(16) 8979-84. doi:10.1073/pnas.151103798 pmid:11481469. PubMed HubMed [VanAalten2001]
3. Horn SJ, Sørbotten A, Synstad B, Sikorski P, Sørlie M, Vårum KM, and Eijsink VG. Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens. FEBS J 2006 Feb; 273(3) 491-503. doi:10.1111/j.1742-4658.2005.05079.x pmid:16420473. PubMed HubMed [Horn2006]
4. Horn SJ, Sikorski P, Cederkvist JB, Vaaje-Kolstad G, Sørlie M, Synstad B, Vriend G, Vårum KM, and Eijsink VG. Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides. Proc Natl Acad Sci U S A 2006 Nov 28; 103(48) 18089-94. doi:10.1073/pnas.0608909103 pmid:17116887. PubMed HubMed [Hornb2006]
5. Zakariassen H, Aam BB, Horn SJ, Vårum KM, Sørlie M, and Eijsink VG. Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency. J Biol Chem 2009 Apr 17; 284(16) 10610-7. doi:10.1074/jbc.M900092200 pmid:19244232. PubMed HubMed [Zakariassen2009]
6. Hoell IA, Dalhus B, Heggset EB, Aspmo SI, and Eijsink VG. Crystal structure and enzymatic properties of a bacterial family 19 chitinase reveal differences from plant enzymes. FEBS J 2006 Nov; 273(21) 4889-900. doi:10.1111/j.1742-4658.2006.05487.x pmid:17010167. PubMed HubMed [Hoell2006]
7. Heggset EB, Hoell IA, Kristoffersen M, Eijsink VG, and Vårum KM. Degradation of chitosans with chitinase G from Streptomyces coelicolor A3(2): production of chito-oligosaccharides and insight into subsite specificities. Biomacromolecules 2009 Apr 13; 10(4) 892-9. doi:10.1021/bm801418p pmid:19222164. PubMed HubMed [Heggset2009]
8. Eijsink VG, Vaaje-Kolstad G, Vårum KM, and Horn SJ. Towards new enzymes for biofuels: lessons from chitinase research. Trends Biotechnol 2008 May; 26(5) 228-35. doi:10.1016/j.tibtech.2008.02.004 pmid:18367275. PubMed HubMed [Eijsink2008]
9. Vaaje-Kolstad G, Houston DR, Riemen AH, Eijsink VG, and van Aalten DM. Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21. J Biol Chem 2005 Mar 25; 280(12) 11313-9. doi:10.1074/jbc.M407175200 pmid:15590674. PubMed HubMed [Kolstad2005]
10. Vaaje-Kolstad G, Horn SJ, van Aalten DM, Synstad B, and Eijsink VG. The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation. J Biol Chem 2005 Aug 5; 280(31) 28492-7. doi:10.1074/jbc.M504468200 pmid:15929981. PubMed HubMed [Kolstadb2005]
11. Vaaje-Kolstad G, Bunaes AC, Mathiesen G, and Eijsink VG. The chitinolytic system of Lactococcus lactis ssp. lactis comprises a nonprocessive chitinase and a chitin-binding protein that promotes the degradation of alpha- and beta-chitin. FEBS J 2009 Apr; 276(8) 2402-15. pmid:19348025. PubMed HubMed [Kolstad2009]