Blar i forfatter "Eijsink, Vincent"

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    • 1H, 13C, 15N resonance assignment of the apo form of the small, chitin-active lytic polysaccharide monooxygenase JdLPMO10A from Jonesia denitrificans 

      Christensen, Idd Andrea; Eijsink, Vincent; Aachmann, Finn Lillelund; Courtade, Gaston (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-11-19)
      The lytic polysaccharide monooxygenase <i>Jd</i>LPMO10A is the N-terminal domain of the multimodular protein Jd1381. The isolated <i>Jd</i>LPMO10A domain is one of the smallest chitin-active lytic polysaccharide monooxygenases known to date with a size of only 15.5 kDa. <i>Jd</i>LPMO10A is a copper-dependent oxidative enzyme that depolymerizes chitin by hydroxylating the C1 carbon in the glycosidic ...

    • Biochemical and structural characterisation of a family GH5 cellulase from endosymbiont of shipworm P. megotara 

      Junghare, Madan; Manavalan, Tamilvendan; Fredriksen, Lasse; Leiros, Ingar; Altermark, Bjørn; Eijsink, Vincent; Vaaje-Kolstad, Gustav (Journal article; Tidsskriftartikkel; Peer reviewed, 2023-04-04)
      Background Cellulases play a key role in the enzymatic conversion of plant cell-wall polysaccharides into simple and economically relevant sugars. Thus, the discovery of novel cellulases from exotic biological niches is of great interest as they may present properties that are valuable in the biorefning of lignocellulosic biomass. Results We have characterized a glycoside hydrolase 5 (GH5) domain ...

    • Discovery and characterization of a thermostable two-domain GH6 endoglucanase from a compost metagenome 

      Jensen, Marianne Slang; Fredriksen, Lasse; Mackenzie, Alasdair; Pope, Phillip; Leiros, Ingar; Chylenski, Piotr; Williamson, Adele Kim; Christopeit, Tony; Østby, Heidi; Vaaje-Kolstad, Gustav; Eijsink, Vincent (Journal article; Tidsskriftartikkel; Peer reviewed, 2018-05-24)
      Enzymatic depolymerization of recalcitrant polysaccharides plays a key role in accessing the renewable energy stored within lignocellulosic biomass, and natural biodiversities may be explored to discover microbial enzymes that have evolved to conquer this task in various environments. Here, a metagenome from a thermophilic microbial community was mined to yield a novel, thermostable cellulase, named ...

    • The lytic polysaccharide monooxygenase CbpD promotes Pseudomonas aeruginosa virulence in systemic infection 

      Askarian, Fatemeh; Uchiyama, Satoshi; Masson, Helen; Sørensen, Henrik Vinther; Golten, Ole; Bunæs, Anne Cathrine; Mekasha, Sophanit; Røhr, Åsmund Kjendseth; Kommedal, Eirik Garpestad; Ludviksen, Judith Anita; Arntzen, Magnus Øverlie; Schmidt, Benjamin; Zurich, Raymond H.; Van Sorge, Nina M.; Eijsink, Vincent; Krengel, Ute; Mollnes, Tom Eirik; Lewis, Nathan E.; Nizet, Victor; Vaaje-Kolstad, Gustav (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-02-23)
      The recently discovered lytic polysaccharide monooxygenases (LPMOs), which cleave polysaccharides by oxidation, have been associated with bacterial virulence, but supporting functional data is scarce. Here we show that CbpD, the LPMO of <i>Pseudomonas aeruginosa</i>, is a chitin-oxidizing virulence factor that promotes survival of the bacterium in human blood. The catalytic activity of CbpD was ...

    • Metagenomics of the Svalbard Reindeer Rumen Microbiome Reveals Abundance of Polysaccharide Utilization Loci 

      Pope, Phillip B; Mackenzie, Alasdair; Gregor, Ivan; Smith, Wendy; Sundset, Monica Alterskjær; McHardy, Alice; Morrison, Mark; Eijsink, Vincent (Journal article; Tidsskriftartikkel; Peer reviewed, 2012)
      Lignocellulosic biomass remains a largely untapped source of renewable energy predominantly due to its recalcitrance and an incomplete understanding of how this is overcome in nature. We present here a compositional and comparative analysis of metagenomic data pertaining to a natural biomass-converting ecosystem adapted to austere arctic nutritional conditions, namely the rumen microbiome of Svalbard ...

    • Structural and functional variation of chitin-binding domains of a lytic polysaccharide monooxygenase from Cellvibrio japonicus 

      Madland, Eva; Forsberg, Zarah; Wang, Yong; Lindorff-Larsen, Kresten; Niebisch, Axel; Modregger, Jan; Eijsink, Vincent; Aachmann, Finn Lillelund; Courtade, Gaston (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-08-17)
      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 cleavage of glycosidic bonds in polysaccharides such as cellulose and chitin. Several LPMOs contain carbohydrate-binding modules (CBMs) that are known to promote LPMO efficiency. ...

    • Structural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae 

      Mazurkewich, Scott; Helland, Ronny; Mackenzie, Alasdair; Eijsink, Vincent; Pope, Phillip Byron; Brändén, Gisela; Larsbrink, Johan (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-08-13)
      Chitin is one of the most abundant renewable organic materials found on earth. The chitin utilization locus in <i>Flavobacterium johnsoniae</i>, which encodes necessary proteins for complete enzymatic depolymerization of crystalline chitin, has recently been characterized but no detailed structural information on the enzymes was provided. Here we present protein structures of the <i>F. johnsoniae</i> ...

    • Structure and function of a CE4 deacetylase isolated from a marine environment 

      Tuveng, Tina Rise; Rothweiler, Ulli; Udatha, D.B.R.K. Gupta; Vaaje-Kolstad, Gustav; Smalås, Arne O.; Eijsink, Vincent (Journal article; Tidsskriftartikkel; Peer reviewed, 2017-11-06)
      Chitin, a polymer of β(1–4)-linked N-acetylglucosamine found in e.g. arthropods, is a valuable resource that may be used to produce chitosan and chitooligosaccharides, two compounds with considerable industrial and biomedical potential. Deacetylating enzymes may be used to tailor the properties of chitin and its derived products. Here, we describe a novel CE4 enzyme originating from a marine ...

    • Visible light-exposed lignin facilitates cellulose solubilization by lytic polysaccharide monooxygenases 

      Kommedal, Eirik; Angeltveit, Camilla Fløien; Klau, Leesa Jane; Ayuso-Fernandez, Ivan; Arstad, Bjørnar; Antonsen, Simen; Stenstrøm, Yngve; Ekeberg, Dag; Gírio, Francisco; Carvalheiro, Florbela; Horn, Svein Jarle; Aachmann, Finn Lillelund; Eijsink, Vincent (Journal article; Tidsskriftartikkel; Peer reviewed, 2023-02-24)
      Lytic polysaccharide monooxygenases (LPMOs) catalyze oxidative cleavage of crystalline polysaccharides such as cellulose and are crucial for the conversion of plant biomass in Nature and in industrial applications. Sunlight promotes microbial conversion of plant litter; this effect has been attributed to photochemical degradation of lignin, a major redox-active component of secondary plant cell walls ...