Characterization of a novel cold-adapted GH1 β-glucosidase from and its application in the hydrolysis of soybean isoflavone glycosides.

The novel β-glucosidase gene () of glycoside hydrolase (GH) family 1 from the psychrotrophic bacterium sp. PB01 was successfully expressed in BL21 (DE3). The deduced PgBgl1 contained 447 amino acid residues with a calculated molecular mass of 51.

Characterization of a Novel Hyperthermophilic GH1 β-Glucosidase from sp. and Its Application in the Hydrolysis of Soybean Isoflavone Glycosides.

A putative β-glucosidase gene, , was amplified from sp. through metagenome database sampling from a hot spring in Yellowstone National Park. BglAc is composed of 485 amino acid residues and bioinformatics analysis showed that it belongs to the GH1 family of β-glucosidases.

[Expression and characterization of mesophilic GH1 β-glucosidase CdBglA from acidophilic ].

β-glucosidase has important applications in food, pharmaceutics, biomass conversion and other fields, exploring β-glucosidase with strong adaptability and excellent properties thus has received extensive interest. In this study, a novel glucosidase from the GH1 family derived from was cloned, expressed, and characterized, aiming to find a better β-glucosidase. The amino acid sequences of GH1 family glucosidase derived from were obtained from the NCBI database, and a recombinant plasmid pET-30a(+)-CdBglA was constructed.