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  • Action of AA9 lytic polysaccharide monooxygenase enzymes . . .
    We investigated the action of two LPMO enzymes from Podospora anserina: Pa LPMO9E and Pa LPMO9H, both containing a CBM1 module Pa LPMO9E preferentially cleaves cellulose at the C1 position, and PaLPMO9H mainly attacks at the C4 position together with some C1 oxidation
  • LPMO AfAA9_B and Cellobiohydrolase AfCel6A from A . . .
    We characterized a cellobiohydrolase (AfCel6A) and lytic polysaccharide monooxygenase LPMO (AfAA9_B) from Aspergillus fumigatus after they were expressed in Pichia pastoris and purified The biochemical parameters suggested that the enzymes were stable; the optimal temperature was ~60 °C
  • LPMO AfAA9_B and Cellobiohydrolase AfCel6A from A . . .
    Here, we present the biochemical characterization of Af Cel6A and Af AA9_B after they are expressed in Pichia pastoris We will show that supplementation of enzymatic cocktails can enhance the production of fermentable sugars, and that LPMOs have a critical role in biomass hydrolysis
  • LPMO AfAA9_B and Cellobiohydrolase AfCel6A from A . . .
    LPMO AfAA9_B and Cellobiohydrolase AfCel6A from A fumigatus Boost Enzymatic Saccharification Activity of Cellulase Cocktail
  • LPMO AfAA9_B and Cellobiohydrolase AfCel6A from A . . .
    We characterized a cellobiohydrolase (AfCel6A) and lytic polysaccharide monooxygenase LPMO (AfAA9_B) from A fumigatus after they were expressed in Pichia pastoris and purified The biochemical parameters suggested that the enzymes were stable; the optimal temperature was ~60 °C
  • Synergistic Action of a Lytic Polysaccharide Monooxygenase . . .
    The combined overexpression of LPMO and CBH1 provided a significantly more efficient cellulase cocktail with an enhanced saccharification performance on PWS under high-level substrate loading
  • LPMO Af AA9_B and Cellobiohydrolase Af Cel6A from A . . .
    We characterized a cellobiohydrolase (AfCel6A) and lytic polysaccharide monooxygenase LPMO (AfAA9_B) from Aspergillus fumigatus after they were expressed in Pichia pastoris and purified The biochemical parameters suggested that the enzymes were stable; the optimal temperature was ~60 C





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