期刊
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
卷 113, 期 -, 页码 233-250出版社
HUMANA PRESS INC
DOI: 10.1385/ABAB:113:1-3:233
关键词
cellulose; cellulase; beta-glucosiclase; Orpinomyces; cellobiase
资金
- Intramural FDA HHS [FD999999] Funding Source: Medline
A beta-glucosidase (Bg1A, EC 3.2.1.21) gene from the polycentric anaerobic fungus Orpinomyces PC-2 was cloned and sequenced. The enzyme containing 657 amino acid residues was homologous to certain animal, plant, and bacterial beta-glucosidases but lacked significant similarity to those from aerobic fungi. Neither cellulose- nor protein-binding domains were found in BgIA. When expressed in Saccharomyces cerevisiae, the enzyme was secreted in two forms with masses of about 110 kDa and also found in two forms associated with the yeast cells. K-m and V-max values of the secreted Bg1A were 0.762 mM and 8.20 mumol/(min(.)mg), respectively, with p-nitrophenyl-beta-D-glucopyranoside (pNPG) as the substrate and 0.310 mM and 6.45 mumol/(min(.)mg), respectively, for the hydrolysis of cellobiose. Glucose competitively inhibited the hydrolysis of pNPG with a K-i of 3.6 mM. beta-Glucosidase significantly enhanced the conversion of cellulosic materials into glucose by Trichoderma reesei cellulase preparations, demonstrating its potential for use in biofuel and feedstock chemical production.
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