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Fig. 11 | Biotechnology for Biofuels

Fig. 11

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. 11

Substrate-binding residue F256 presents a specific orientation in D2-BGL relative to that in AaBGL1. The W–F–Y triad (in stick form) acts as substrate-binding subsite +1 in D2-BGL (in blue) and in Aspergillus aculeatus β-glucosidase AaBGL1 (in grey). TCB thiocellobiose

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Biotechnology for Biofuels and Bioproducts

ISSN: 2731-3654

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