Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cranberry pomace contains large amounts of phenolic glycosides, which are important sources of free phenolics that have many food uses such as antioxidants, flavorings, and nutraceuticals. Our hypothesis was that these glycosides in cranberry pomace could be hydrolyzed by beta-glucosidase produced by Lentinus edodes during solid-state fermentation. On the basis of this hypothesis, our objective was to investigate the potential of using cranberry pomace as a substrate for the production of free phenolics and beta-glucosidase through solid-state fermentation by a food-grade fungus L. edodes. Our results suggested that L. edodes beta-glucosidase played a major role in release of phenolic aglycons from cranberry pomace during solid-state fermentation. After 50 days of cultivation, the yield of total free phenolics reached the maximum of 0.5 mg per g of pomace, while the beta-glucosidase activity was about 9 units per g of pomace. The enzyme exhibited optimal activity at 60 degrees C and at pH 3.5 and was stable at temperatures up to 50 degrees C and between pH 3 and 6.5. The major free phenolics produced from cranberry pomace were identified by HPLC as gallic acid, chlorogenic acid, p-hydroxybenzoic acid, and p-coumaric acid. These results suggest that cranberry pomace is a potential substrate for producing food-grade phenolics and fungal beta-glucosidase. The L. edodes beta-glucosidase showed good stability and tolerance to low pH and, therefore has potential applications in wine and juice processing for aroma and flavor enrichment through enzymatic hydrolysis of glucoside precursors.
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PMID:Solid-state bioconversion of phenolics from cranberry pomace and role of Lentinus edodes beta-glucosidase. 1072 70

An extracellular tannase was produced from solid-state cultures of Aspergillus niger. The enzyme was purified to homogeneity from the cell-free culture broth by preparative isoelectric focusing and by FPLC using anion-exchange and gel-filtration chromatography. SDS-PAGE analysis as well as gel localization studies of purified tannase indicated the presence of two enzyme forms, with molecular masses of 90 kDa and 180 kDa. The tannase had an isoelectric point of 3.8, a temperature optimum of 60-70 degrees C and a pH optimum of 6.0. The substrate specificity of the tannase was determined by HPLC analysis of tannin substrates and products. The enzyme was able to remove gallic acid from both condensed and hydrolysable tannins. Internal sequences were obtained from each of the gel-purified and trypsin-digested tannase forms. The peptide sequences obtained from both forms were identical to sequences within a beta-glucosidase from Aspergillus kawachii. The purified tannase was tested for beta-glucosidase activity and was shown to hydrolyse cellobiose efficiently. However, no beta-glucosidase activity was detected when the enzyme was assayed in the presence of tannic acid.
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PMID:A novel tannase from Aspergillus niger with beta-glucosidase activity. 1452 26