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Cellulose is the most abundant polysaccharide in lignocellulosic biomass, where it is interlinked with lignin and hemicellulose. Bioethanol can be produced from biomass. Since breaking down biomass is difficult, cellulose-active enzymes secreted by filamentous fungi play an important role in degrading recalcitrant lignocellulosic biomass. We characterized a cellobiohydrolase ( Af Cel6A) and lytic polysaccharide monooxygenase LPMO ( Af AA9_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. Further characterization revealed high turnover numbers ( k cat  of 147.9 s -1 and 0.64 s -1 , respectively). Surprisingly, when combined, Af Cel6A and Af AA9_B did not act synergistically. Af Cel6A and Af AA9_B association inhibited Af Cel6A activity, an outcome that needs to be further investigated. However, Af Cel6A or Af AA9_B addition boosted the enzymatic saccharification activity of a cellulase cocktail and the activity of cellulase Af -EGL7. Enzymatic cocktail supplementation with Af Cel6A or Af AA9_B boosted the yield of fermentable sugars from complex substrates, especially sugarcane exploded bagasse, by up to 95%. The synergism between the cellulase cocktail and Af AA9_B was enzyme- and substrate-specific, which suggests a specific enzymatic cocktail for each biomass by up to 95%. The synergism between the cellulase cocktail and Af AA9_B was enzyme- and substrate-specific, which suggests a specific enzymatic cocktail for each biomass.

LPMO AfAA9_B and Cellobiohydrolase AfCel6A from A. fumigatus Boost Enzymatic Saccharification Activity of Cellulase Cocktail