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Fig. 10 | Biotechnology for Biofuels

Fig. 10

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. 10

Pichia pastoris-expressed recombinant D2-BGL exhibits variable hypermannosylation. a Yeast-expressed D2-BGL is highly mannosylated (line 5). Peptide N-glycosidase F (PNGase F, lines 1 and 2) and endo-glucosidase H (Endo H, lines 3 and 4) can remove N-glycans from Pichia pastoris-expressed D2-BGL under denaturing conditions (heating at 100 °C for 10 min) (lines 1 and 4). b N-Glycans were removed by endoglycosidase H (Endo H) treatment at 37 °C for 4 h

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Biotechnology for Biofuels and Bioproducts

ISSN: 2731-3654

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