Gene/Protein Disease Symptom Drug Enzyme Compound
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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)

Enzymatic glycosidation of twenty-one kinds of alcohols (n-hepanol, n-octanol, 2-phenylethanol, 3-phenylpropanol, 4-phenylbutanol, 5-phenylpentanol, 6-phenylhexanol, furfury alcohol, 2-pyridinemethanol, isobutanol, isopentanol, p-methoxycinnamylalcohol) including secondary alcohols (isopropanol, cyclohexanol, 1-phenylethanol) and 1,omega-alkanediols (1,5-pentanediol, 1,6-hexanediol, 1,7-heptanediol, 1,8-octanediol, 1,9-nonanediol), salicyl alcohol and 4-nitrophenyl beta-D-glucopyranoside (5) using beta-glucosidase from almonds stereoselectively gave the corresponding beta-D-glucopyranosides in moderate yield.
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PMID:Simple synthesis of beta-D-glycopyranosides using beta-glycosidase from almonds. 1475 17

A beta-glucosidase was purified from the digestive fluid of the palm weevil Rhynchophorus palmarum L. (Coleoptera: Curculionidae) by chromatography on anion-exchange, gel filtration, and hydrophobic interaction columns. The preparation was shown to be homogeneous on polyacrylamide gels, beta-glucosidase is a monomeric protein with a molecular weight of 58 kDa based on its mobility in SDS-PAGE and 60 kDa based on gel filtration. Maximal beta-glucosidase activity occurred at 55 degrees C and pH 5.0. The purified beta-glucosidase was stable at 37 degrees C and its pH stability was in the range of 5.0-6.0. The enzyme readily hydrolyzed p-nitrophenyl-beta-D-glucoside, cellobiose, cellodextrins and required strictly beta-gluco configuration for activity. It cleaved glucose-glucose beta-(1-4) linkages better than beta-(1-2), beta-(1-3) and beta-(1-6) linkages. The catalytic efficiency (K(cat)/K(M)) values for p-nitrophenyl-beta-D-glucoside and cellobiose were respectively 240.48 mM(-1)s(-1) and 134.80 mM(-1)s(-1). Beta-glucosidase was capable of catalysing transglucosylation reactions. The yield of glucosylation of 2-phenylethanol (20 %), catalysed by the beta-glucosidase in the presence of cellobiose as glucosyl donor, is lower than those reported previously with conventional sources of beta-glucosidases. In addition, the optimum pH is different for the hydrolysis (pH 5.0) and transglucosylation reactions (pH 6.6).
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PMID:Purification and biochemical characterization of a specific beta-glucosidase from the digestive fluid of larvae of the palm weevil, Rhynchophorus palmarum. 1961 Dec 39