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)

The hydrolysis of purified celluloses (cotton, Avicel, Cellulose-123, Solka Floc SW40) and cellulosic wastes (rice straw, sugarcane bagasse, wood powders, paper factory effluents) by Sclerotium rolfsii CPC 142 culture filtrate was studied. Factors which effect saccharification such as pH, temperature, enzyme concentration, substrate concentration, produce inhibition, adsorption, and inactivation of enzyme and particle size were studied. Virtually no inhibition (less than 3%) of cellulose hydrolysis by the culture filtrate was observed by cellobiose and glucose up to 100 mg/mL. Filter paper degrading enzyme(s) (but neither carboxymethylcellulase nor beta-glucosidase) was adsorbed on cellulose. The n value in the S. rolfsii system was calculated to be 0.32 for Avicel P.H. 101 and 0.53 for alkali-treated (AT) rice straw indicating penetration of cellulase into AT rice straw. In batch experiments at 10% substrate level, solutions containing 6 to 7%, 3.8 to 4.7%, 4.0 to 5.1%, and 4.2 to 4.9% reducing sugars were produced in 24 to 48 from AT rice straw. AT bagasse, alkali - peracetic acid treated mesta wood and paper factory sedimented sludge effluent, respectively. The main constituent in the hydrolysate from cellulose was glucose with little or no cellobiose, probably due to the high cellobiase content in the culture filtrate.
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PMID:Enzymatic hydrolysis of cellulosic materials by Sclerotium rolfsii culture filtrate for sugar production. 3 98

1,4-beta-D-Glucan glucohydrolase (exo-1,4-beta-D-glucosidase) (EC 3.2.1.74) was isolated from growth supernatants of Torulopsis wickerhamii and was subjected to hydrodynamic, optical (CD), and kinetic analysis after purification to homogeneity by ammonium sulfate precipitation, size exclusion chromatography, ion exchange chromatography, and isopycnic banding centrifugation in cesium chloride. The last step was found to separate the enzyme from strongly associating, high molecular weight polysaccharide. Enzyme homogeneity was established by isoelectric focusing, sodium dodecyl sulfate-gel electrophoresis, and analytical high performance size exclusion chromatography using dual detection. The native exo-1,4-beta-D-glucosidase was found to be a dimer of 151,000 +/- 21,100 daltons by high performance size exclusion chromatography and 143,600 +/- 1,800 daltons by sedimentation equilibrium. The enzyme has a 12% linked carbohydrate content (mostly mannose) and no essential metal ions. Hydrolysis of p-nitrophenyl-beta-D-glucopyranoside was found to be optimal at pH 4.25 and 50 degrees C. The enzyme was found to produce beta-D-glucose from cellodextrins (indicating retention of anomeric configuration during hydrolysis) and demonstrated depolymerization from the non-reducing polymer terminus. The enzyme followed competitive type inhibition with p-nitrophenyl-beta-D-glucopyranoside as substrate and demonstrated high values of Ki for D-glucose and D-cellobiose inhibition (190 and 230 mM, respectively). The exo-1,4-beta-D-glucosidase was found to hydrolyze cellotetraose more rapidly than D-cellobiose and aryl-beta-D-glycosides more rapidly than all other substrates. Low levels of activity were found for the polymeric substrates beta-glucan (yeast cell walls), Avicel, and Walseth cellulose. Although this enzyme demonstrates broad disaccharide substrate specificity, a characteristic common to beta-D-glucosidases from many sources, the ability to hydrolyze higher cellodextrins more rapidly than cellobiose renders this enzyme the first exo-1,4-beta-D-glucosidase purified from yeast.
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PMID:Isolation and characterization of a 1,4-beta-D-glucan glucohydrolase from the yeast, Torulopsis wickerhamii. 309 75

The induction of endo-1,4-beta-glucanase synthesis by Trichoderma reesei QM 9414 was investigated in conidia, mycelia and protoplasts. Cellulose induced endoglucanase synthesis only in conidia, but not in glucose-grown mycelia or protoplasts. Cellooligosaccharides and sophorose induced endoglucanase synthesis in mycelia, conidia and protoplasts. Only conidia exhibited detectable basal endoglucanase levels, whereas beta-glucosidase activity was found in conidia, mycelia and protoplasts. The beta-glucosidase was inhibited in vitro by nojirimycin and glucono-delta-lactone. Addition of either of these inhibitors to the induction medium blocked de noro synthesis of endo-1,4-beta-glucanase with cellulose (conidia) or cellooligosaccharides (protoplasts and mycelia) as inducer, whereas induction by sophorose remained unaffected. The results are consistent with the assumption that basal constitutive levels of endoglucanase and beta-glucosidase are involved in the induction of cellulase synthesis by cellulose in T. reesei.
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PMID:Involvement of a conidial endoglucanase and a plasma-membrane-bound beta-glucosidase in the induction of endoglucanase synthesis by cellulose in Trichoderma reesei. 311 61

Cellulose-acetate gel electrophoresis, a technique commonly used for the separation of human acid hydrolases, was applied to study heterogeneity in acid beta-glucosidase (EC 3.2.1.45). With this technique, three forms of beta-glucosidase were distinguishable in extracts of several tissues. The most anodic beta-glucosidase activity (band 3) represents the broad-specificity beta-glucosidase that is not deficient in Gaucher disease and is not inhibited by conduritol B-epoxide (CBE). The beta-glucosidase activity was deficient in Gaucher disease. A third beta-glucosidase activity with an intermediate mobility (band 2) was also inhibited by CBE and deficient in Gaucher disease. Band 1 and band 2 beta-glucosidase thus represent different forms of glucocerebrosidase. By adding phosphatidylserine and sphingolipid activator protein (SAP-2), monomeric glucocerebrosidase could be completely converted into a form that comigrated with band 2 beta-glucosidase of tissue extracts. The addition of phosphatidylserine only also resulted in a changed mobility of the monomeric enzyme, but the migration in this case differed from that of band 2 beta-glucosidase of tissue extracts. The electrophoretic profile of beta-glucosidase activity of tissue extracts changed upon ethanol/chloroform extraction: the two glucocerebrosidase forms were converted into a band with a mobility identical to that of band 1 beta-glucosidase. Our findings indicate that the interaction of glucocerebrosidase with phospholipid and SAP-2 has major effects on the mobility of the enzyme in the cellulose-acetate gel electrophoresis system. The findings with the cellulose-acetate gel electrophoretic system are discussed in relation to the heterogeneity in glucocerebrosidase observed with sucrose density gradient analysis, immunochemical methods and isoelectric focussing studies.
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PMID:Heterogeneity in human acid beta-glucosidase revealed by cellulose-acetate electrophoresis. 313 Jan 6

Microcrystalline cellulose (10 mg of Avicel/ml) was hydrolysed to glucose by different concentrations of the purified cellulase components endoglucanase (EG) II and cellobiohydrolases (CBH) I and II, alone and in combination with each other, in the presence of excess beta-glucosidase. At a concentration of 360 micrograms/ml (160 micrograms of EG II/ml, 100 micrograms of CBH I/ml and 100 micrograms of CBH II/ml) the degree of synergism among them was negligible. As the concentration of cellulase decreased, the degree of synergism increased, reaching an optimum at 20 micrograms/ml (5 micrograms of EG II/ml, 10 micrograms of CBH I/ml and 5 micrograms of CBH II/ml). There was no apparent relationship between the ratio of the components and the degree of synergism. The latter is probably due, though it could not be proved, to the level of saturation of the substrate with each component. Inhibition of Avicel hydrolysis was observed when the substrate was incubated with saturating and nonsaturating concentrations of a mixture of EG II and CBH I respectively. A similar result was also observed with a combination of EG I and EG II.
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PMID:The role of cellulase concentration in determining the degree of synergism in the hydrolysis of microcrystalline cellulose. 259 Jan 59

Nineteen fungi were isolated from different soil samples on the basis of clear zones formed on Rose Bengal Cellulose agar medium. In shake flasks th isolate K1 gave 12.1 units/ml of CMCase activity. A mutant of the isolate K1, KM7, was selected after N-methyl-N'-nitro-N-nitrosoguanidine treatment of the wild-type. This mutant differed morphologically from the parent strain on RBCA medium and gave 36.2 units/ml of CMCase activity which represented about 50% of the enzyme yield from the standard organism, Trichoderma viride QM 9414 (80 units/ml of CMCase activity). The isolate K1, which was identified as a Phoma species, produced 48 units of beta-glucosidase. The yield of beta-glucosidase was increased about 8-fold in the mutant KM7 and was about 68% higher than the level found in T. viride QM 9414.
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PMID:Isolation and mutation of cellulolytic fungi. 678 15

The production of beta-glucosidase by Aspergillus terreus was investigated in liquid shake cultures. Enzyme production was maximum on the 7th day of growth (2.18 U/ml) with the initial pH of the medium in the range of 4.0-5.5. Cellulose (Sigmacell Type 100) at 1.0% (wt/vol) gave maximum beta-glucosidase activity among the various soluble and insoluble carbon sources tested. Potassium nitrate was a suitable nitrogen source for enzyme production. Triton X-100 at 0.15% (vol/vol) increased the enzyme levels of A. terreus. The test fungal strain showed an ability to ferment glucose to ethanol.
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PMID:Production of beta-glucosidase by Aspergillus terreus. 776 52

A novel fungal beta-glucosidase gene (bgl4) and its homologue (bgl2) were cloned from the cellulolytic fungi Humicola grisea and Trichoderma reesei, respectively. The deduced amino acid sequences of H. grisea BGL4 and T. reesei BGL2 comprise 476 and 466 amino acids, respectively, and share 73.1% identity. These beta-glucosidases show significant homology to plant beta-glucosidases belonging to the beta-glucosidase A (BGA) family. Both genes were expressed in Aspergillus oryzae, and the recombinant beta-glucosidases were purified. Recombinant H. grisea BGL4 is a thermostable enzyme compared with recombinant T. reesei BGL2. In addition to beta-glucosidase activity, recombinant H. grisea BGL4 showed a significant level of beta-galactosidase activity, while recombinant T. reesei BGL2 showed weak beta-galactosidase activity. Cellulose saccharification by Trichoderma cellulases was improved by the addition of recombinant H. grisea BGL4.
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PMID:Molecular cloning and expression of the novel fungal beta-glucosidase genes from Humicola grisea and Trichoderma reesei. 1010 Dec 86

The effect of fructooligosaccharides (FOS) on cecal enzyme activity was studied. Adult male Wistar rats were fed a fiber-free diet supplemented with 5% cellulose, a 5% mixture (1:1) of cellulose and FOS or 5% FOS as a source of fiber for 4 weeks. The cecal content was used to measure azoreductase, beta-glucuronidase, beta-glucosidase, nitrate reductase and nitroreductase activities. Cellulose-fed diet increased significantly body weight gain, food intake and fecal stool weight compared to FOS-fed diet. No differences in food intake between FOS-containing diets were found. FOS-containing diets showed statistically higher weight of cecal content and weight of cecal wall compared with the cellulose group. There were significant differences in cecal enzyme activities between cellulose-fed rats and FOS-fed rats. Cellulose-FOS-fed diet decreased significantly nitroreductase, beta-glucuronidase and beta-glucosidase enzymes, but did not differ statistically in azoreductase and nitrate reductase compared with the control group. FOS-fed diet increased significantly reductive enzymes and decreased hydrolytic enzymes compared with the cellulose group. The incorporation of cellulose in diet seems to affect the prebiotic effect of FOS, since both cellulose and FOS are possible substrates for bifidobacteria proliferation. The results suggest that a mixture of cellulose and FOS as a source of dietary fiber could have a healthier effect on bacterial enzyme activities than each type of dietary fiber alone.
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PMID:Effect of short-chain fructooligosaccharides and cellulose on cecal enzyme activities in rats. 1246 25

A comprehensive mechanistic kinetic model for enzymatic degradation of cotton fibers has been established based on a complete factorial experiment in combination with multivariate stepwise regression analysis. The analysis of the statistical parameter value in the model suggests that the enzymatic degradation of cotton fiber is a progressive and heterogeneous process that includes, at least, two courses that occur sequentially and then progress in parallel. Cellulose fibers were first depolymerized or solubilized by the synergism between cellobiohydrolase I (CBHI) and endoglucanase I (EGI), and then the oligomers obtained were randomly hydrolyzed into glucose by EGI and beta-glucosidase. The proposed model can be applied to the quantitative estimation of the effects of three cellulase components, CBHI, EGI, and beta-glucosidase separately, or in combination during the entire process of cellulose degradation. The validity of the proposed model has been verified by a filter paper activity assay. Its other applicability was also discussed.
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PMID:Quantitative estimate of the effect of cellulase components during degradation of cotton fibers. 1498 Aug 25


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