M
Morten Sørlie
Researcher at Norwegian University of Life Sciences
Publications - 22
Citations - 4287
Morten Sørlie is an academic researcher from Norwegian University of Life Sciences. The author has contributed to research in topics: Processivity & Chitin. The author has an hindex of 18, co-authored 18 publications receiving 3711 citations. Previous affiliations of Morten Sørlie include Norwegian University of Science and Technology.
Papers
More filters
Journal ArticleDOI
An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides.
Gustav Vaaje-Kolstad,Bjørge Westereng,Svein Jarle Horn,Zhanliang Liu,Hong Zhai,Morten Sørlie,Vincent G. H. Eijsink +6 more
TL;DR: An enzyme is described that acts on the surface of crystalline chitin, where it introduces chain breaks and generates oxidized chain ends, thus promoting further degradation by chit inases, demonstrating the existence of a hitherto unknown enzyme activity.
Journal ArticleDOI
Production of Chitooligosaccharides and Their Potential Applications in Medicine
Berit Bjugan Aam,Ellinor Bævre Heggset,Anne Line Norberg,Morten Sørlie,Kjell M. Vårum,Vincent G. H. Eijsink +5 more
TL;DR: Techniques that may be used to produce and characterize reasonably well-defined CHOS fractions are provided and possible medical applications of CHOS are presented, including tumor growth inhibition and inhibition of TH2-induced inflammation in asthma and use as a bone-strengthener in osteoporosis.
Journal ArticleDOI
Cleavage of cellulose by a CBM33 protein.
Zarah Forsberg,Gustav Vaaje-Kolstad,Bjørge Westereng,Anne C. Bunæs,Yngve Stenstrøm,Alasdair Mackenzie,Morten Sørlie,Svein Jarle Horn,Vincent G. H. Eijsink +8 more
TL;DR: It is shown that some members of the CBM33 family cleave crystalline cellulose as demonstrated by chromatographic and mass spectrometric analyses of soluble products released from Avicel or filter paper on incubation with CelS2, a CBM 33‐containing protein from Streptomyces coelicolor A3(2).
Journal ArticleDOI
Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides
Svein Jarle Horn,Pawel Sikorski,Jannicke B. Cederkvist,Gustav Vaaje-Kolstad,Morten Sørlie,Bjørnar Synstad,Gert Vriend,Kjell M. Vårum,Vincent G. H. Eijsink +8 more
TL;DR: The present results show that this processivity comes at a large cost in terms of enzyme speed, so it might be better to focus strategies for enzymatic depolymerization of polysaccharide biomass on improving substrate accessibility for nonprocessive enzymes rather than on improving the properties of processive enzymes.
Journal ArticleDOI
The chitinolytic machinery of Serratia marcescens – a model system for enzymatic degradation of recalcitrant polysaccharides
TL;DR: The catalytic mechanisms of these enzymes as well as the structural basis of each enzyme's specific role in the chitin degradation process are discussed, and how knowledge of this enzyme system may be extrapolated to other enzyme systems for conversion of insoluble polysaccharides is discussed.