Characterization of a Beta-glucosidase from Bacillus Licheniformis and Its Effect on Bioflocculant Degradation

Overview

Journal AMB Express

Date 2017 Nov 8

PMID 29110104

Citations 8

Authors

Zhen Chen

Tong Meng

Zhipeng Li

Peize Liu

Yuanpeng Wang

Ning He

Dafeng Liang

Affiliations

Soon will be listed here.

Abstract

Bacillus licheniformis CGMCC 2876, an aerobic spore-forming bacterium, produces a polysaccharide bioflocculant that is biodegradable and harmless. The present study determined that β-glucosidase played a negative role in bioflocculant synthesis. The gene encoding β-glucosidase was cloned and expressed in Escherichia coli BL21. This gene consists of 1437 bp and encodes 478 amino acid residues. The recombinant β-glucosidase (Bgl.bli1) was purified and showed a molecular mass of 53.4 kDa by SDS-PAGE. The expression and reaction conditions of Bgl.bli1 were optimized; the activity of β-glucosidase reached a maximum at 45.44 U/mL. Glucose clearly inhibited the activity of β-glucosidase. The purified recombinant Bgl.bli1 hydrolysed polysaccharide bioflocculant in vitro and synergised with other cellulases. The ability of Bgl.bli1 to hydrolyse polysaccharide bioflocculant was the reason for the decrease in flocculating activity and indicated the utility of this enzyme for diverse industrial processes.

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