• 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 ...
    • 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, ...
    • Human Chitotriosidase: Catalytic Domain or Carbohydrate Binding Module, Who’s Leading HCHT’s Biological Function 

      Crasson, Oscar; Courtade, Gaston; Leonard, Raphael R; Aachmann, Finn Lillelund; Legrand, Francois; Parente, Raffaella; Baurain, Denis; Galleni, Moreno; Sørlie, Morten; Vandevenne, Marylene (Journal article; Peer reviewed, 2017)
      Chitin is an important structural component of numerous fungal pathogens and parasitic nematodes. The human macrophage chitotriosidase (HCHT) is a chitinase that hydrolyses glycosidic bonds between the N-acetyl-D-glucosamine ...
    • 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 ...
    • 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 (Journal article; Peer reviewed, 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)
      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 ...
    • Ny giv, et tiltak mot frafall i videregående opplæring 

      Sørlie, Morten (Master thesis, 2011)
      Frafall i videregående opplæring er et stort samfunnsproblem. En tredjedel fra hvert årskull slutter årlig i videregående opplæring. I denne sammenheng iverksatte regjeringen vinteren 2011 det statlige ...
    • 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 ...