Z
Zarah Forsberg
Researcher at Norwegian University of Life Sciences
Publications - 35
Citations - 2588
Zarah Forsberg is an academic researcher from Norwegian University of Life Sciences. The author has contributed to research in topics: Chitin & Cellulase. The author has an hindex of 20, co-authored 35 publications receiving 1883 citations. Previous affiliations of Zarah Forsberg include Swedish University of Agricultural Sciences & Novozymes.
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Journal ArticleDOI
Oxidative cleavage of polysaccharides by monocopper enzymes depends on H2O2.
Bastien Bissaro,Bastien Bissaro,Åsmund K. Røhr,Gerdt Müller,Piotr Chylenski,Morten Skaugen,Zarah Forsberg,Svein Jarle Horn,Gustav Vaaje-Kolstad,Vincent G. H. Eijsink +9 more
TL;DR: The use of H2O2 by a monocopper enzyme that is otherwise cofactor-free offers new perspectives regarding the mode of action of copper enzymes, and these findings have implications for the enzymatic conversion of biomass in Nature and in industrial biorefining.
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
Structural and functional characterization of a conserved pair of bacterial cellulose-oxidizing lytic polysaccharide monooxygenases.
Zarah Forsberg,Alasdair Mackenzie,Morten Sørlie,Åsmund K. Røhr,Ronny Helland,Andrew S. Arvai,Gustav Vaaje-Kolstad,Vincent G. H. Eijsink +7 more
TL;DR: The structural and functional characterization of two functionally coupled cellulose-active LPMOs belonging to auxiliary activity family 10 (AA10) that commonly occur in cellulolytic bacteria are described, concluding that substrate specificity depends not on copper site architecture, but rather on variation in substrate binding and orientation.
Journal ArticleDOI
A rapid quantitative activity assay shows that the Vibrio cholerae colonization factor GbpA is an active lytic polysaccharide monooxygenase.
Jennifer S. M. Loose,Zarah Forsberg,Marco W. Fraaije,Vincent G. H. Eijsink,Gustav Vaaje-Kolstad +4 more
TL;DR: A method for quantification of C1‐oxidized chitooligosaccharides (aldonic acids) and hence LPMO activity is described, used to quantify the activity of a four‐domain L PMO from Vibrio cholerae, GbpA, which is a virulence factor with no obvious role in biomass processing.
Journal ArticleDOI
Structural diversity of lytic polysaccharide monooxygenases
TL;DR: The number of available LPMO structures has increased rapidly, including the first structure of an enzyme-substrate complex and the insights gained are reviewed below.