Browsing NTNU Open by Author "Eijsink, Vincent"
Now showing items 1-14 of 14
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1H, 13C, 15N resonance assignment of the chitin-active lytic polysaccharide monooxygenase BlLPMO10A from Bacillus licheniformis
Courtade, Gaston; Balzer, Simone; Forsberg, Zarah; Vaaje-Kolstad, Gustav; Eijsink, Vincent; Aachmann, Finn Lillelund (Journal article; Peer reviewed, 2015)The chitin-active 19.2 kDa lytic polysaccharide monooxygenase BlLPMO10A from Bacillus licheniformis has been isotopically labeled and recombinantly expressed. In this paper, we report the 1H, 13C, 15N resonance assignment ... -
A C4-oxidizing lytic polysaccharide monooxygenase cleaving both cellulose and cello-oligosaccharides
Isaksen, Trine; Westereng, Bjørge; Aachmann, Finn Lillelund; Agger, Jane; Kracher, Daniel; Kittl, Roman; Ludwig, R.; Haltrich, Dietmar; Eijsink, Vincent; Horn, Svein Jarle (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 ... -
Analytical Tools for Characterizing Cellulose-Active Lytic Polysaccharide Monooxygenases (LPMOs)
Westereng, Bjørge; Loose, Jennifer Sarah Maria; Vaaje-Kolstad, Gustav; Aachmann, Finn Lillelund; Sørlie, Morten; Eijsink, Vincent (Journal article; Peer reviewed, 2018)Lytic polysaccharide monooxygenases are copper-dependent enzymes that perform oxidative cleavage of glycosidic bonds in cellulose and various other polysaccharides. LPMOs acting on cellulose use a reactive oxygen species ... -
Backbone and side-chain 1H, 13C, and 15N chemical shift assignments for the apo-form of the lytic polysaccharide monooxygenase NcLPMO9C
Courtade, Gaston; Wimmer, Reinhard; Dimarogona, Maria; Sandgren, Mats; Eijsink, Vincent; Aachmann, Finn Lillelund (Journal article; Peer reviewed, 2016)The apo-form of the 23.3 kDa catalytic domain of the AA9 family lytic polysaccharide monooxygenase NcLPMO9C from Neurospora crassa has been isotopically labeled and recombinantly expressed in Pichia pastoris. In this paper, ... -
Centre for Digital Life Norway - Annual report 2017
Johansen, Finn-Eirik; Brautaset, Trygve; Aune, Marie Hjelmseth; Patriksson, Alexandra; Falkenberg, Liv Eggset; Kleppe, Rune; Dick, Gunnar; Strand, Berit Løkensgard; Eijsink, Vincent; Røyne, Anja; Goksøyr, Anders; Svendsen, John Sigurd Mjøen; Fyhn, Marianne; Vik, Jon Olav; Wentzel, Alexander; Aksnes, Astrid; Bruheim, Per; Carlsen, Sven Magnus; Åm, Heidrun (Research report, 2018) -
Human chitotriosidase-catalyzed hydrolysis of chitosan
Eide, Kristine Bistrup; Norberg, Anne Line; Heggset, Ellinor Bævre; Lindbom, Anne Rita; Vårum, Kjell Morten; Eijsink, Vincent; Sørlie, Morten (Journal article; Peer reviewed, 2012)Chitotriosidase (HCHT) is one of two family 18 chitinases produced by humans, the other being acidic mammalian chitinase (AMCase). The enzyme is thought to be part of the human defense mechanism against fungal parasites, ... -
Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase
Courtade, Gaston; Wimmer, Reinhard; Kjendseth, Åsmund Røhr; Preims, Marita; Felice, Alfons K.G.; Dimarogona, Maria; Vaaje-Kolstad, Gustav; Sørlie, Morten; Sandgren, Mats; Ludwig, Roland; Eijsink, Vincent; Aachmann, Finn Lillelund (Journal article; Peer reviewed, 2016)Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze oxidative cleavage of glycosidic bonds using molecular oxygen and an external electron donor. We have used NMR and isothermal titration ... -
Mechanistic basis of substrate–O2 coupling within a chitin-active lytic polysaccharide monooxygenase: An integrated NMR/EPR study
Courtade, Gaston; Ciano, Luisa; Paradisi, Alessandro; Lindley, Peter J.; Forsberg, Zarah; Sørlie, Morten; Wimmer, Reinhard; Davies, Gideon J.; Eijsink, Vincent; Walton, Paul H.; Aachmann, Finn Lillelund (Peer reviewed; Journal article, 2020)Lytic polysaccharide monooxygenases (LPMOs) have a unique ability to activate molecular oxygen for subsequent oxidative cleavage of glycosidic bonds. To provide insight into the mode of action of these industrially important ... -
NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions
Aachmann, Finn Lillelund; Sørlie, Morten; Skjåk-Bræk, Gudmund; Eijsink, Vincent; Vaaje-Kolstad, Gustav (Journal article; Peer reviewed, 2012)Lytic polysaccharide monooxygenases currently classified as carbohydrate binding module family 33 (CBM33) and glycoside hydrolase family 61 (GH61) are likely to play important roles in future biorefining. However, the ... -
Polysaccharide degradation by lytic polysaccharide monooxygenases
Forsberg, Zarah; Sørlie, Morten; Petrovic, Dejan; Courtade, Gaston; Aachmann, Finn Lillelund; Vaaje-Kolstad, Gustav; Bissaro, Bastien; Kjendseth, Åsmund Røhr; Eijsink, Vincent (Journal article; Peer reviewed, 2019)The discovery of oxidative cleavage of glycosidic bonds by enzymes currently known as lytic polysaccharide monooxygenases (LPMOs) has had a major impact on our current understanding of the enzymatic conversion of recalcitrant ... -
Production, characterization, and application of an alginate lyase, AMOR_PL7A, from hot vents in the Arctic mid-ocean ridge
Vuoristo, Kiira; Fredriksen, Lasse; Oftebro, Maren; Arntzen, Magnus Øverlie; Aarstad, Olav Andreas; Stokke, Runar; Steen, Ida Helene; Hansen, Line Degn; Schüller, Reidar Barfod; Aachmann, Finn Lillelund; Horn, Svein Jarle; Eijsink, Vincent (Peer reviewed; Journal article, 2019)Enzymatic depolymerization of seaweed polysaccharides is gaining interest for the production of functional oligosaccharides and fermentable sugars. We describe a thermostable alginate lyase belonging to Polysaccharide Lyase ... -
Resonance assignments for the apo-form of the cellulose-active lytic polysaccharide monooxygenase TaLPMO9A
Kitaoku, Yoshihito; Courtade, Gaston; Petrovic, Dejan; Fukamizo, Tamo; Eijsink, Vincent; Aachmann, Finn Lillelund (Journal article; Peer reviewed, 2018)The apo-form of the 24.4 kDa AA9 family lytic polysaccharide monooxygenase TaLPMO9A from Thermoascus aurantiacus has been isotopically labeled and recombinantly expressed in Pichia pastoris. In this paper, we report the ... -
Simultaneous analysis of C1 and C4 oxidized oligosaccharides, the products of lytic polysaccharide monooxygenases acting on cellulose
Westereng, Bjørge; Arntzen, Magnus Øverlie; Aachmann, Finn Lillelund; Varnai, Aniko; Eijsink, Vincent; Wittrup Agger, Jane (Journal article; Peer reviewed, 2016)Lytic polysaccharide monooxygenases play a pivotal role in enzymatic deconstruction of plant cell wall material due to their ability to catalyze oxidative cleavage of glycosidic bonds. LPMOs may release different products, ... -
The carbohydrate-binding module and linker of a modular lytic polysaccharide monooxygenase promote localized cellulose oxidation
Courtade, Gaston; Forsberg, Zarah; Heggset, Ellinor Bævre; Eijsink, Vincent; Aachmann, Finn Lillelund (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 ...