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)

Esculin has been incorporated into both a medium and test with 20% bile for many years to differentiate Bacteroides from Fusobacterium organisms. After 24 to 48 h, all members of the Bacteroides fragilis group grow in 20% bile and hydrolyze esculin. Fusobacterium mortiferum can both grow in bile and hydrolyze esculin, thus limiting the use of the bile-esculin medium and test. The hypothesis that constitutive esculinase (beta-glucosidase) could differentiate Bacteroides from Fusobacterium organisms was investigated. Clinical isolates and American Type Culture Collection clones of the B. fragilis group and other species of Bacteroides and Fusobacterium were tested. All B. fragilis were positive within 30 min. In no case was a Fusobacterium organism positive for constitutive enzyme in a hydrolyzable substrate-based test. The percentage of positive results for other species of Bacteroides agreed with those published in the literature for the esculin test. The genus Fusobacterium can be separated from Bacteroides organisms based on a lack of constitutive beta-glucosidase in the former in a 30-min one-tube test.
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PMID:Lack of constitutive beta-glucosidase (esculinase) in the genus Fusobacterium. 393 May 63

Ten Basidiobolus ranarum (= Basidiobolus haptosporus) strains, isolated from faeces of 102 different lower vertebrates (ectotherms) exhibited in Antwerp Zoo, or from their environment were studied for their temperature requirements, haemolysis and other enzyme activities in vitro. All isolates grew well at 25 and 37 degrees C. Three strains that produced undulated zygospore walls were haemolytic and positive for hyaluronidase. All the isolates produced urease, N-acetyl-beta-glucosaminidase, trypsin, lipase, lecithinase, gelatinase, collagenase and elastase, but failed to produce amylase, keratinase and beta-glucosidase. Three isolates failed to produce phosphatase. Only one strain failed to produce DNase. Aesculin was not hydrolysed. Chitinase activity was inconclusive. The results of this study illustrate the importance of exotic animals kept in temperate regions as carriers of potentially pathogenic organisms. In addition to the morphological characteristics, the identification can be based on enzymatic profiles. Enzymatic activity detection may help to explain the pathogenic mechanism of the fungus.
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PMID:Isolation of Basidiobolus ranarum from ectotherms in Antwerp zoo with special reference to characterization of the isolated strains. 1042 99

More than seventy strains of aerobic bacteria showing beta-glucosidase activity were isolated from a ginseng field, using a newly designed Esculin-R2A agar, and identified by their 16S rRNA gene sequences. Of these microorganisms, twelve strains could convert the major ginsenoside, Rb(1), to the pharmaceutically active minor ginsenoside Rd. Three strains, Burkholderia pyrrocinia GP16, Bacillus megaterium GP27 and Sphingomonas echinoides GP50, were phylogenetically studied, and observed to be most potent at converting ginsenoside Rb(1) almost completely within 48 h, as shown by TLC and HPLC analyses.
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PMID:Microbial conversion of major ginsenoside rb(1) to pharmaceutically active minor ginsenoside rd. 1627 39

Exploring new beta-glucosidase genes is of great importance to industrialize beta-glucosidase. The genomes of Aspergillus fumigatus contain a bgl gene, which encodes a 65 kDa putative beta-glucosidase. The bgl gene was cloned into an expression plasmid and transformed to Escherichia coli BL21 (DE3). The bgl was expressed upon induction of Isopropyl beta-D-1-thiogalactopyranoside (IPTG). The recombinant protein was purified by GST-tag affinity chromatography. The purified recombinant Bgl was characterized using Esculin as substrate. The optimum temperature and pH were 45 degrees C and 5.0-6.0, respectively. The K(m) for Esculin was 17.7 mmol/L. The enzyme was stable in the range of pH 4-7. After incubation at 70 degrees C for 2 h, the recombinant Bgl remained 60% of its activity. Metal ions and chemical reagents had different influences on the activity of beta-glucosidase. Ca2+ (1 mmol/L) could increase enzyme activity slightly. On the contrary, the enzyme activity was greatly inhibited by 5 mmol/L Sodium dodecyl sulfate (SDS). Based on our results, the A. fumigatus Bgl was thermostable beta-glucosidase.
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PMID:[Cloning, expression and characterization of beta-glucosidase from Aspergillus fumigatus]. 2440 88