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, 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. (2000). Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-A resolution. Proc Natl Acad Sci U S A. 2000;97(11):5842-7. DOI:10.1073/pnas.97.11.5842 |
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, Sørbotten A, Synstad B, Sikorski P, Sørlie M, Vårum KM, and Eijsink VG. (2006). Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens. FEBS J. 2006;273(3):491-503. DOI:10.1111/j.1742-4658.2005.05079.x |
4. 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 |
5. 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 |
7. Heggset EB, Hoell IA, Kristoffersen M, Eijsink VG, and Vårum KM. (2009). Degradation of chitosans with chitinase G from Streptomyces coelicolor A3(2): production of chito-oligosaccharides and insight into subsite specificities. Biomacromolecules. 2009;10(4):892-9. DOI:10.1021/bm801418p |
8. Eijsink VG, Vaaje-Kolstad G, Vårum KM, and Horn SJ. (2008). Towards new enzymes for biofuels: lessons from chitinase research. Trends Biotechnol. 2008;26(5):228-35. DOI:10.1016/j.tibtech.2008.02.004 |
9. Vaaje-Kolstad G, Houston DR, Riemen AH, Eijsink VG, and van Aalten DM. (2005). Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21. J Biol Chem. 2005;280(12):11313-9. DOI:10.1074/jbc.M407175200 |
10. Vaaje-Kolstad G, Horn SJ, van Aalten DM, Synstad B, and Eijsink VG. (2005). The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation. J Biol Chem. 2005;280(31):28492-7. DOI:10.1074/jbc.M504468200 |
11. Vaaje-Kolstad G, Bunaes AC, Mathiesen G, and Eijsink VG. (2009). 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;276(8):2402-15. DOI:10.1111/j.1742-4658.2009.06972.x |