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Fig. 4 | Biotechnology for Biofuels

Fig. 4

From: Engineering a highly active thermophilic β-glucosidase to enhance its pH stability and saccharification performance

Fig. 4

Sequence, structure and molecular mass analyses of wild type and mutant Bgl3A proteins. a The amino acid sequences of wild type and mutant enzymes with potential O-glycosylation sites (http://www.cbs.dtu.dk/services/NetOGlyc/) indicated. b Modeled Bgl3A with Cel3A of H. jecorina (PDB: 3ZYZ) as the template. The potential glycosylated residues are shown in balls. c SDS–PAGE analysis of the wild type and mutant enzymes produced in P. pastoris and treated with/without PNGase F. Lanes M, the standard protein molecular weight markers; 1 the purified Bgl3A; 2 the N-deglycosylated Bgl3A; 3 the purified M1; 4 the N-deglycosylated M1; 5 the purified M2; 6 the N-deglycosylated M2

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