Characterization of a novel β-glucosidase from a compost microbial metagenome with strong transglycosylation activity.

ABSTRACT: The β-glucosidase encoded by the td2f2 gene was isolated from a compost microbial metagenomic library by functional screening. The protein was identified to be a member of the glycoside hydrolase family 1 and was overexpressed in Escherichia coli, purified, and biochemically characterized. The recombinant β-glucosidase, Td2F2, exhibited enzymatic activity with β-glycosidic substrates, with preferences for glucose, fucose, and galactose. Hydrolysis occurred at the nonreducing end and in an exo manner. The order of catalytic efficiency for glucodisaccharides and cellooligosaccharides was sophorose > cellotetraose > cellotriose > laminaribiose > cellobiose > cellopentaose > gentiobiose, respectively. Intriguingly, the p-nitrophenyl-β-D-glucopyranoside hydrolysis activity of Td2F2 was activate

SUBMITTER: Uchiyama T 

PROVIDER: S-EPMC3689974 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature