Blar i Institutt for bioteknologi og matvitenskap på tidsskrift "Journal of Biological Chemistry"
Viser treff 1-7 av 7
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A C4-oxidizing lytic polysaccharide monooxygenase cleaving both cellulose and cello-oligosaccharides
(Journal article; Peer reviewed, 2014)Lignocellulosic biomass is a renewable resource that significantly can substitute fossil resources for the production of fuels, chemicals, and materials. Efficient saccharification of this biomass to fermentable sugars ... -
The effect of linker conformation on performance and stability of a two-domain lytic polysaccharide monooxygenase
(Journal article; Peer reviewed, 2023)A considerable number of lytic polysaccharide monooxygenases (LPMOs) and other carbohydrate-active enzymes are modular, with catalytic domains being tethered to additional domains, such as carbohydrate-binding modules, by ... -
The Natural Product Domain Seeker version 2 (NaPDoS2) webtool relates ketosynthase phylogeny to biosynthetic function
(Peer reviewed; Journal article, 2022)The Natural Product Domain Seeker (NaPDoS) webtool detects and classifies ketosynthase (KS) and condensation domains from genomic, metagenomic, and amplicon sequence data. Unlike other tools, a phylogeny-based classification ... -
Structural and functional aspects of mannuronic acid–specific PL6 alginate lyase from the human gut microbe Bacteroides cellulosilyticus
(Journal article; Peer reviewed, 2019)Alginate is a linear polysaccharide from brown algae consisting of 1,4-linked β-D-mannuronic acid (M) and α-L-guluronic acid (G) arranged in M, G, and mixed MG blocks. Alginate was assumed to be indigestible in humans, but ... -
Structural and functional characterization of the R-modules in alginate C-5 epimerases AlgE4 and AlgE6 from Azotobacter vinelandii
(Journal article; Peer reviewed, 2014)The bacterium Azotobacter vinelandii produces a family of seven secreted and calcium-dependent mannuronan C-5 epimerases (AlgE1–7). These epimerases are responsible for the epimerization of β-d-mannuronic acid (M) to ... -
Structural and functional variation of chitin-binding domains of a lytic polysaccharide monooxygenase from Cellvibrio japonicus
(Peer reviewed; Journal article, 2021)Among the extensive repertoire of carbohydrate-active enzymes, lytic polysaccharide monooxygenases (LPMOs) have a key role in recalcitrant biomass degradation. LPMOs are copper-dependent enzymes that catalyze oxidative ... -
The carbohydrate-binding module and linker of a modular lytic polysaccharide monooxygenase promote localized cellulose oxidation
(Journal article; Peer reviewed, 2018)Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze the oxidative cleavage of polysaccharides such as cellulose and chitin, a feature that makes them key tools in industrial biomass ...