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Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The bglA gene, encoding a beta-glucosidase from Bacillus polymyxa, has been expressed in Saccharomyces cerevisiae under control of the CYC-GAL promoter inducible by galactose. The expression of bglA-encoded activity in the strain used as a host was not sufficient to allow its growth with cellobiose as a carbon source. However, a recessive mutation in a gene designated cem1 has been obtained which, combined with the expression of beta-glucosidase activity, allows the growth of S. cerevisiae on cellobiose. The expression of the blgA gene in a cem1 strain confers on S. cerevisiae the capability for an efficient fermentation of cellobiose, as detected by the formation of CO2.
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PMID:Construction of a Saccharomyces cerevisiae strain able to ferment cellobiose. 193 17

The bglA gene which encodes a beta-glucosidase from Bacillus polymyxa, has been expressed in Saccharomyces cerevisiae under control of the yeast CYC-GAL promoter. Strains have been constructed which carry the gene in different locations: in a multicopy plasmid, a single integration at the URA3 locus, or multiple integrations at the RDN1 locus. Integrative transformation at RDN1 yielded genetically stable clones with a high level of beta-glucosidase activity. Coordinated overexpression of the GAL4 inducer protein further increased the level of enzyme activity, although eventually caused the lysis of the cultures. Diploid, triploid and tetraploid strains derived from the transformants with multiple integrations were constructed and expression of beta-glucosidase activity in different conditions of growth was assayed. While per-cell activity increased with ploidy, specific activity was about the same in strains of equivalent genotype regardless of ploidy. Genetically stable and regulated expression in Saccharomyces of beta-glucosidase activity is interesting for the development of strains able to ferment beta-glycosidic sugars (i.e. cellobiose and lactose). From another point of view, the bglA product proved to be a convenient reporter enzyme to monitor heterologous gene expression.
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PMID:Induced expression of bacterial beta-glucosidase activity in Saccharomyces. 759 43

The mutagenic effects of rutin and quercetin have aroused the interest of many investigators. To develop the microbial degradation of rutin, a thermophilic actinomycete, which could hydrolyze rutin, was isolated from compost soil. The taxonomical characteristics of this thermophilic actinomycete were examined and identified as Thermoactinomyces vulgaris PU18-2. After cultivation of T. vulgaris PU18-2 in the rutin-CYC medium for 60 h, the culture filtrate had a rutin-degrading ability, but the cell-free extract did not. There was no quercetin, rutinose, rhamnose, and glucose accumulated in the rutin hydrolysate of the culture filtrate. Both alpha-rhamnosidase and beta-glucosidase activities were not found in the culture filtrate of the T. vulgaris PU18-2 in the rutin-CYC medium. These results showed that the initial attack on rutin by the extracellular enzymes of T. vulgaris PU18-2 apparently was not through the glycosidase-mediated hydrolysis of glycosidic bond.
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PMID:Degradation of rutin by Thermoactinomyces vulgaris and other thermophilic compost isolates. 1948 31