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- Title
LPMO Af AA9_B and Cellobiohydrolase Af Cel6A from A. fumigatus Boost Enzymatic Saccharification Activity of Cellulase Cocktail.
- Authors
Bernardi, Aline Vianna; Gerolamo, Luis Eduardo; de Gouvêa, Paula Fagundes; Yonamine, Deborah Kimie; Pereira, Lucas Matheus Soares; de Oliveira, Arthur Henrique Cavalcante; Uyemura, Sérgio Akira; Dinamarco, Taisa Magnani
- Abstract
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 (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. Further characterization revealed high turnover numbers (kcat of 147.9 s−1 and 0.64 s−1, respectively). Surprisingly, when combined, AfCel6A and AfAA9_B did not act synergistically. AfCel6A and AfAA9_B association inhibited AfCel6A activity, an outcome that needs to be further investigated. However, AfCel6A or AfAA9_B addition boosted the enzymatic saccharification activity of a cellulase cocktail and the activity of cellulase Af-EGL7. Enzymatic cocktail supplementation with AfCel6A or AfAA9_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 AfAA9_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 AfAA9_B was enzyme- and substrate-specific, which suggests a specific enzymatic cocktail for each biomass.
- Subjects
CELLULOSE 1,4-beta-cellobiosidase; CELLULASE; PICHIA pastoris; TURNOVER frequency (Catalysis); ASPERGILLUS fumigatus
- Publication
International Journal of Molecular Sciences, 2021, Vol 22, Issue 1, p276
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms22010276