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

ABSTRACT:

Background

β-Glucosidase is an important member of the biomass-degrading enzyme system, and plays vital roles in enzymatic saccharification for biofuels production. Candidates with high activity and great stability over high temperature and varied pHs are always preferred in industrial practice. To achieve cost-effective biomass conversion, exploring natural enzymes, developing high level expression systems and engineering superior mutants are effective approaches commonly used.

Results

A newly identified β-glucosidase of GH3, Bgl3A, from Talaromyces leycettanus JCM12802, was overexpressed in yeast strain Pichia pastoris GS115, yielding a crude enzyme activity of 6000 U/ml in a 3 L fermentation tank. The purified enzyme exhibited outstanding enzymatic properties, including f

SUBMITTER: Xia W 

PROVIDER: S-EPMC4955127 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature