Browsing Brage NMBU by Author "Sørlie, Morten"
Now showing items 21-40 of 54
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Initial characterization of an iron superoxide dismutase from Thermobifida fusca
Hamre, Anne Grethe; Al-Sadawi, Rim; Johannesen, Kirsti Merete; Bisarro, Bastien; Kjendseth, Åsmund Røhr; Leiros, Hanna-Kirsti S.; Sørlie, Morten (Peer reviewed; Journal article, 2023) -
Innledende kinetikkstudier av den lytisk polysakkarid monooksygenasen, SmAA10A, ved bruk av stopped-flow spektrofotometri og isotermisk titreringskalorimetri
Thorpe, James Alexander Ydstebø (Master thesis, 2021)De kobberavhengige enzymene kjent som lytisk polysakkarid monooksygenaser (LPMO-er) katalyserer den oksidative nedbrytningen av polysakkarider som kitin og cellulose ved spalting av glykosidbindinger. Under denne prosessen ... -
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) -
An investigation of the interplay between in situ hydrogen peroxide production and catalytic efficiency in lytic polysaccharide monooxygenase reactions
Stepnov, Anton (PhD thesis;2022:27, Doctoral thesis, 2022)Lytic polysaccharide monooxygenases (LPMOs) are mono-copper enzymes that catalyze oxidative depolymerization of recalcitrant carbohydrate substrates, such as chitin and cellulose. LPMOs have received much attention from ... -
Kinetic investigations of the oxidative cleavage of oligomeric carbohydrates provide novel insights into the catalytic action of fungal lytic polysaccharide monooxygenases
Rieder, Lukas (PhD Thesis;2021:61, Doctoral thesis, 2021)The lytic polysaccharide monooxygenases (LPMOs) are a recently discovered class of redoxactive mono-copper enzymes that catalyze the oxidative cleavage of glycosidic bonds in recalcitrant plant or chitin-based biomass, ... -
Kinetic relationships with processivity in Serratia marcescens family 18 glycoside hydrolases
Hamre, Anne Grethe; Sørlie, Morten (Peer reviewed; Journal article, 2019)In nature, recalcitrant polysaccharides such as chitin and cellulose are degraded by glycoside hydrolases (GH) that act synergistically through different modes of action including attack from reducing-end and nonreducing-end ... -
Kitin depolymerisering og selektiv hydrokarbonoksidasjon : enzymatisk foredling av naturressurser
Gustavsen, Daniel (Master thesis, 2017)Kitin er et polysakkarid bestående av N-acetylglukosamin enheter som kobles sammen med β(1→4) glykosidbindinger. CBP21, en lytisk polysakkarid monooksygenase (LPMO), bryter glykosidbindinger i kitinpolymeren med en oksidativ ... -
Ligninvalorisering ved bruk av enzymatiske cocktailer
Trondsen, Susann (Master thesis, 2018)Planters biomasse består i hovedsak av cellulose, hemicellulose og lignin, der lignin utgjør 15-40 % av plantens tørrvekt. Lignin er den nest mest forekommende polymeren på landjorda. Den er svært heterogen, avledet fra ... -
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) -
Molecular evolution of the substrate specificity of bacterial lytic polysaccharide monooxygenases (LPMOs)
Bjølgerud, Helene (Master thesis, 2018)The transition to a more environment-friendly economy has spurred the research on how to efficiently convert recalcitrant polysaccharides into soluble sugars. One of the major breakthroughs in the field has been the discovery ... -
NMR and fluorescence spectroscopies reveal the preorganized binding site in family 14 carbohydrate-binding module from human chitotriosidase
Madland, Eva; Crasson, Oscar; Vandevenne, Marylene; Sørlie, Morten; Aachmann, Finn Lillelund (Peer reviewed; Journal article, 2019): Carbohydrate-binding modules (CBM) play important roles in targeting and increasing the concentration of carbohydrate active enzymes on their substrates. Using NMR to get the solution structure of CBM14, we can gain ... -
NMR and fluorescence spectroscopies reveal the preorganized binding site in family 14 carbohydrate-binding module from human chitotriosidase
Madland, Eva; Crasson, Oscar; Vandevenne, Marylene; Sørlie, Morten; Aachmann, Finn Lillelund (Peer reviewed; Journal article, 2019)Carbohydrate-binding modules (CBM) play important roles in targeting and increasing the concentration of carbohydrate active enzymes on their substrates. Using NMR to get the solution structure of CBM14, we can gain insight ... -
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) -
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 (Peer reviewed; Journal article, 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 ... -
Processivity and substrate-binding in family 18 chitinases
Sørlie, Morten; Zakariassen, Henrik; Norberg, Anne Line; Eijsink, Vincent (Journal article; Peer reviewed, 2012) -
Processivity, substrate positioning, and binding: The role of polar residues in a family 18 glycoside hydrolase
Hamre, Anne Grethe; Suvamay, Jana; Reppert, Nicole; Payne, Christina M.; Sørlie, Morten (Journal article; Peer reviewed, 2015) -
Roles of charged residues in the active site of Lytic Polysaccharide Monooxygenase : effect on catalysis
Karlsen, Victoria (Master thesis, 2017)Lytic Polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze the oxidative cleavage of glycosidic bonds in polysaccharides in the presence of H2O2 or molecular oxygen paired with a reductant. LPMOs ... -
The roles of conserved second sphere residues in lytic polysaccharide monooxygenase catalysis
Mollatt, Maja (Master thesis, 2022)The demand for sustainable and renewable options to generate energy and materials is increasing as we become more aware of the environmental impact of a petroleum-based economy. Biomass may be employed as a sustainable ... -
Rollen til aromatiske residuer i det aktive setet under substratdegradering
Strømnes, Anne-Grethe Skaarberg (Master thesis, 2016-08-10)Denne oppgaven er skrevet som en større del av et forskningsprosjekt, der målet er å tilegne seg kunnskap om enzymatisk nedbrytning av det uløselige karbohydratet kitin. Denne biopolymeren er den nest mest vanlige naturen, ... -
Slow off-rates and strong product binding are required for processivity and efficient degradation of recalcitrant chitin by family 18 chitinases
Kurasin, Mihhail; Kuusk, Silja; Kuusk, Piret; Sørlie, Morten; Väljamäe, Priit (Journal article; Peer reviewed, 2015)