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)

Forty strains of bacilli were isolated from flat sour evaporated milk and were characterized as Bacillus stearothermophilus (5 strains), Bacillus licheniformis (10 strains), Bacillus coagulans (15 strains), Bacillus macerans (5 strains), and Bacillus subtilis (5 strains). The hydrolases of these strains were examined with the API ZYM system, and the ability of these strains to produce acid in milk incubated at different temperatures was also examined. Esterase, esterase lipase, lipase, valine aminopeptidase, phosphoamidase, beta-glucuronidase, and beta-glucosidase were the activities found in all strains tested; they were strain-dependent and ranged between 1 and 5 by the API ZYM test. The same strains produced various concentrations of acid in milk. These organisms may be responsible for the flat sour spoilage in evaporated milk.
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PMID:Biochemical activities of Bacillus species isolated from flat sour evaporated milk. 143 Apr 75

Phenotypic characteristics of 100 strains pertaining to the group of mesophilic aeromonas isolated in feces of patients with diarrhea (23 A. hydrophila, 34 A. sobria, 19 A. caviae, and 24 considered atypical because produced a the negative esculin reaction and a positive gas formation from glucose [TSI]). The percentages obtained in the different biochemical tests support the hypothesis that in this group there is a taxonomic complexity. We observed variations in the following tests: LDC, arabinose, Voges-Proskauser, lactose, and motility and hemolytic activity. We compared manual and automatic procedures in detecting esculinase and beta-galactosidase activity (ONPG). The study of constitutional enzymatic activity by means of API ZYM system can not be used to differentiate the distinct species although the enzyme beta-glucosidase is detected preferentially in A. hydrophila.
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PMID:[Phenotypic characteristics of 100 strains belonging to the mesophilic aeromonas group isolated from feces]. 190 54

The production of patulin and griseofulvin by 49 different isolates of Penicillium griseofulvum Dierckx was analyzed by high-performance liquid chromatography. Eleven isolates were obtained from pistachio nuts, 37 were obtained from wheat seeds, and 1 was obtained from the American Type Culture Collection. Activities of 19 enzymes were also assayed by the API ZYM system. From these results it may be deduced that there are two different groups among the strains tested which cannot be distinguished by morphological and cultural characteristics. One group of isolates did not produce detectable amounts of patulin and griseofulvin when grown in sucrose-yeast extract and Wickerham media, while enzymatic activities were quantitatively distinct from the other group, which produced patulin and griseofulvin in variable proportions. Leucine arylamidase, phosphoamidase, and beta-D-glucosidase are the main enzymes with differing activities between the two groups. Differences in physiological characteristics among isolates of a single species reveal shortcomings in the classification of the penicillia based only on morphological criteria. Thus, determination of the ability to yield mycotoxins and antibiotics as well as determination of enzymatic activities appear to be very valuable tools in the taxonomy of these fungi and for food toxicology.
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PMID:Differentiation of Penicillium griseofulvum Dierckx isolates by enzyme assays and by patulin and griseofulvin analyses. 212 9

A total of 32 strains of the family Leptospiraceae (23 strains of Leptospira interrogans, 6 strains of Leptospira biflexa, 2 strains of Leptonema and 1 strain of Leptospira parva) were examined for enzyme activities using 89 substrates (API ZYM system). More than 90% of the strains belonging to the family Leptospiraceae possessed strong activities of beta-D-galactosidase, beta-D-glucosidase and 5 esterases (C5, C6, C8, C9 and C10). More than 90% of the strains belonging to the genus Leptospira, except L. parva, had strong activities of L-lysine arylamidase and alpha-L-glutamate arylamidase. L. biflexa strains, except serovar andamana, were different from the other strains examined in that they possessed glycyl-glycine arylamidase, glycyl-phenylalanine arylamidase and L-tryptophan arylamidase. L. biflexa strains, except andamana, L. parva and Leptonema strains possessed strong activities of glycine arylamidase and leucyl-glycine arylamidase. Two strains of the genus Leptonema were different from the strains belonging to the genus Leptospira in that they possessed strong activities of beta-D-lactosidase. L. parva lacked alpha-D-galactosidase which other strains belonging to the family Leptospiraceae possessed. Dendrogram analysis revealed that strains belonging to the family Leptospiraceae were divided into 4 groups. The first group consisted of all strains belonging to L. interrogans and serovar andamana of L. biflexa; the second group consisted of the remaining 5 serovars of L. biflexa; the third group consisted of the genus Leptonema; and the fourth group consisted of only L. parva.
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PMID:Enzyme activities of the strains belonging to family Leptospiraceae detected by the API ZYM system. 289 26

An enzymatic characterization of 16 strains of Aeromonas species including A. hydrophila (7), A. sobria (5), and A. caviae (4) was carried out using API Peptidase (strips numbered 1, 2, 3, 4, 5, and 6); API Esterase and API "Osidase" test strips. A total of 89 substrates was used in the assay and included 59 arylamides (aminopeptides), 10 esters, and 20 carbohydrates. All three species were remarkably uniform in their reactivities. Nineteen (32%) of the arylamide substrates used were hydrolyzed by all three species. Very strong arylamidase activity was displayed by all three species for L-lysine, L-hydroxyproline, L-arginine, L-alanine, L-proline, and L-leucyl-L-alanine. Esterase activity was strongest against caproate (C6), caprylate (C8), nonanoate (C9), and caprate (C10) substrates. Only a limited number of carbohydrate substrates were hydrolyzed; strong N-acetyl-beta-D-glucosaminidase activity was given by all strains. Both A. hydrophila and A. caviae gave strong beta-D-glucosidase reactivities, while A. sobria appeared to be negative for this enzyme. The results of our preliminary study show that some of the enzymes examined may be useful in the identification and differentiation of these species. The API enzyme assays yielded rapid (4 hr) results. The assays were easy to perform, relatively inexpensive and reproducible. The importance of replicate testing and the inclusion of uninoculated (buffer only) controls as part of the assay is emphasized.
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PMID:Enzymatic characterization of three aeromonas species using API Peptidase, API "Osidase," and API Esterase test kits. 307 50

In this report we attempt to explain the discrepancy between beta-glucosidase (EC 3.2.1.21) activity in Candida albicans as measured by commercial kits and that found in an experimental assay. beta-Glucosidase activity in American and Israeli isolates of C. albicans was evaluated with the API ZYM and YeastIdent systems (Analytab Products) and with experimental biochemical assays. Activity was found with whole cells and cell extracts of isolates from both sources. The greatest beta-glucosidase activity was found at pH 5.0 and with p-nitrophenyl-beta-glucopyranoside (PNP-BDG) as the substrate. In assays with beta-naphthyl-beta-D-glucopyranoside and 6-bromo-2-naphthyl-beta-D-glucopyranoside (6-Br-2-naphthyl-BDG), no enzyme activity was detected in whole cells and only limited activity was found in cell extracts of isolates from both sources. In studies with PNP-BDG at pH 5.0 and 7.5, 29 to 38% less activity was found at both pHs with American whole cells, and minor activity (20%) was found at pH 7.5 with isolates from both sources. Because assays with PNP-BDG in cell extracts of isolates from both sources showed no significant differences in activity, the more limited beta-glucosidase activity in American whole cells was most likely due to less efficient transport. Because the API ZYM system uses 6-Br-2-naphthyl-BDG as the substrate and because the substrate is buffered at pH 7.5 in the API YeastIdent kit, both systems appear to be of limited value for the detection of beta-glucosidase activity in C. albicans.
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PMID:beta-Glucosidase in Candida albicans and its application in yeast identification. 310 12

The enzymatic activities of 53 strains of Pseudomonas cepacia were determined by using the API ZYM system. Strong alkaline phosphatase, acid phosphatase, butyrate esterase, caprylate esterase, myristate lipase, leucine arylamidase, and phosphoamidase activities were consistently detected in all strains. Weak activities were observed for valine arylamidase, beta-glucosidase, and N-acetyl-beta-glucosaminidase. No activities could be demonstrated for cystine arylamidase, trypsin, chymotrypsin, alpha-galactosidase, beta-galactosidase, beta-glucuronidase, alpha-glucosidase, alpha-mannosidase, and alpha-fucosidase. Enzymatic activities of pseudomonads may provide useful information about their pathogenesis and information for identification of Pseudomonas species.
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PMID:Enzymatic characterization of Pseudomonas cepacia by API ZYM profile. 335 98

213 oral isolates of Candida albicans and 62 isolates of C. tropicalis were tested for their hydrolytic enzyme profiles with the API ZYM system. One major biotype accounted for more than 50% of the isolates and a number of minor biotypes was recognized in both Candida species. The enzyme profiles of the major biotypes were identical and one quarter of the C. tropicalis isolates possessed a beta-glucosidase which has not been previously described.
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PMID:Biotypes of oral Candida albicans and Candida tropicalis isolates. 351 80

API ZYM and API An-Ident enzymatic substrate tests were done on six oral species which are difficult to characterize with conventional biochemical tests. "Bacteroides forsythus, the "fusiform" Bacteroides species (A. C. R. Tanner, M. A. Listgarten, M. N. Strzempko, and J. L. Ebersole, manuscript in preparation), is difficult to cultivate in broth media, yet it gave 15 positive tests in these series. The tests were able to separate this new species from species of Capnocytophaga and Fusobacterium. "B. forsythus" reactions were similar but not identical to those of reference Bacteroides species. Positive reactions for alpha-glucosidase, beta-glucosidase, alpha-fucosidase, and alpha-glucuronidase suggest that "B. forsythus" may be saccharolytic. It was the only species tested which was trypsin positive. Wolinella species, Campylobacter concisus, B. gracilis, and Eikenella corrodens are asaccharolytic, and characterization relies heavily on sensitivities to inhibitory agents. These species reacted weakly in the API ZYM and API An-Ident enzymatic substrate tests, and the reactions were not useful for separating these species. The enzyme reactions differentiated Wolinella recta and C. concisus from Selenomonas sputigena, another oral motile but saccharolytic organism.
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PMID:API ZYM and API An-Ident reactions of fastidious oral gram-negative species. 393 May 58

The enzyme activity of the rat hindgut microflora maintained in an anaerobic two-stage continuous culture was compared with that of rat cecal contents. A qualitative comparison (API ZYM) showed a high degree of similarity between the two populations. Quantitative determinations showed that azoreductase, beta-glucosidase, nitrate reductase, and nitroreductase activities were comparable, and that beta-glucuronidase activity was very low in the culture. beta-Glucuronidase, beta-glucosidase, and nitrate reductase activities were induced within the culture by their respective substrates. Bile acids influenced microbial activity in vitro, with cholic acid inducing beta-glucosidase, azoreductase, and beta-glucuronidase activities and decreasing nitrate reductase activity. Chenodeoxycholic acid increased beta-glucosidase and beta-glucuronidase activities and decreased azoreductase, nitrate reductase, and nitroreductase activities in vitro. These studies demonstrate that the rat hindgut microflora may be successfully cultured in vitro and suggest control mechanisms that regulate the metabolic activity of these organisms in vivo.
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PMID:Metabolic activity and enzyme induction in rat fecal microflora maintained in continuous culture. 641 66


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