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Fig. 4 | Biotechnology for Biofuels

Fig. 4

From: Chaetomella raphigera β-glucosidase D2-BGL has intriguing structural features and a high substrate affinity that renders it an efficient cellulase supplement for lignocellulosic biomass hydrolysis

Fig. 4

Cellulase mixtures complemented with the β-glucosidase D2-BGL efficiently hydrolyze acid-pretreated sugarcane bagasse and rice straw. Enzyme amounts are represented by exo-glucanase activity units (for Avicel substrate) for C1.5L, RUT-C30 and CTec3 and by β-glucosidase activity (for pNPG substrate) for D2-BGL. The conversion rate is defined as the total weight of glucose obtained after hydrolysis divided by the total weight of cellulose in the biomass. Experiments were performed in triplicate, and error bars represent the standard deviation

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Biotechnology for Biofuels and Bioproducts

ISSN: 2731-3654

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