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)

Calf pancreas microsomes incorporated radioactively labeled D-glucose from UDP-D-glucose into products extracted with chloroform/methanol (2:1, v/v), chloroform/methanol/water (10:102.5, v/v), and into the residual precipitate, with a pH optimum in Tris/maleate buffer of about 5.3. The chloroform/methanol extract contained a single 14C-labeled acidic product, which was identified as dolichyl beta-D-glucosyl phosphate. It was stable to mild alkali, yielded D-[14C]glucose upon mild acid hydrolysis, and a 14C-labeled compound with the chromatographic mobility of 1,6-anhydro-beta-D-glucopyranosyl upon hot alkali treatment. The [14C]glucolipid had the same chromatographic mobility as dolichyl beta-D-[14C]mannosyl phosphate, and its formation was stimulated by exogenous dolichyl phosphate. The chloroform/methanol/water extract contained radioactive lipid-bound oligosaccharides which were retained on DEAE-cellulose more strongly than dolichyl D-[14C]glucosyl phosphate. They were stable to mild alkali, but labile to acid and hot alkali. Acid treatment yielded a D-glucose-labeled oligosaccharide fraction which was shown by gel filtration to be slightly larger than most of the D-mannose-labeled oligosaccharides. About 80% of the radioactive D-glucose residues could be removed with alpha-glucosidase, but not with beta-glucosidase. Pancreatic dolichyl beta-D-[14C]glucosyl phosphate incubated with calf pancreas microsomes served as direct donor of D-glucosyl residues to lipid-bound oligosaccharides and to the precipitate. These oligosaccharides had the same size as those labeled from UDP-D-[14C]glucose, and the D-[14C]glucose residues could also be removed with alpha-glucosidase.
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PMID:Glucosyltransferase activity in calf pancreas microsomes. Formation of dolichyl D[14C]glucosyl phosphate and 14C-labeled lipid-linked oligosaccharides from UDP-D-[14C]glucose. 84 29

Linamarase (EC 3.2.1.21) was purified from cassava petiole, stem, and root cortex by ammonium sulfate precipitation, column chromatography on Sepharose 6B, and chromatofocusing. The last step resolved the enzyme from each source into three forms with pI values of 4.3, 3.3, and 2.9. Each form was found to be oligomeric, consisting of one kind of subunit, Mr 63,000. The major isozyme with a pI of 4.3 from petiole showed a Km for linamarin of 0.6 mM and possessed both beta-glucosidase and beta-fucosidase activities. The former was sensitive to inhibition by delta-gluconolactone, isopropyl-beta-D-thioglucoside, and HgCl2, whereas the latter was inhibited by Tris ion.
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PMID:Characterization of cyanogenic beta-glucosidase (linamarase) from cassava (Manihot esculenta Crantz). 314 Jul 30

beta-Glucosidase from Saccharomyces lactis strains Y-123 (B(h)), Y-14 (B(m)), and Y-1057A (B(1)) was partially purified. The pH optima, Michaelis constants, and activation energies were determined for the hydrolysis of p-nitro-phenyl-beta-d-glucoside by each of the enzymes. Differences among these constants were not enough to account for the low specific activity of beta-glucosidase in strains Y-14 and Y-1057A. Enzyme-inhibitor constants were measured for a series of alkyl and aryl glucosides. In general, the three enzymes are arylglucosidases. Tris(hydroxymethyl)-aminomethane inhibited all three enzymes in an uncompetitive fashion. The inhibition was antagonized by Mg(++). An antiserum was prepared to the highly purified (200-fold) beta-glucosidase from strain Y-123. The nature and degree of cross-reaction between the three beta-glucosidases was investigated by double diffusion in agar and neutralization tests. Spur formation in the immunodiffusion tests and similar equivalence points in the neutralization tests indicated a strong degree of cross-reaction between the three enzymes. The ratio of enzyme activity to antigenicity was used to compare the relative molecular activity of beta-glucosidase in the three strains. Each strain produced the same amount of beta-glucosidase per milligram of cell protein. The results are consistent either with a lower turnover number for the beta-glucosidase in strains Y-14 and Y-1057A or with the production of beta-glucosidase with a "normal" turnover number and enough cross-reacting material to effectively reduce the specific activity to the observed levels.
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PMID:Comparison of the catalytic and immunological properties of beta-glucosidases from three strains of Saccharomyces lactis. 497 91

This enzyme shows beta-D-glucosidase, beta-D-fucosidase and beta-D-galactosidase activities, all associated in a single peak in Sephadex G-200, DEAE-cellulose, concanavalin A-Sepharose chromatographies, and in high resolution isoelectric focusing (pI 4.56), having the optimal pH in the range 4.5-5.5. The enzyme is very stable under different conditions: (i) at pH in the range 5.5-7.0; (ii) in successive freezing-thawing cycles; (iii) at 4 degrees C; (iv) after exhaustive ultrasonic treatment. It is not stable beyond 40 degrees C, and in the presence of urea, Triton X-100, SDS or mercaptoethanol. HgCl2, KCN, Tris, maltose and the lactones were inhibitors of the enzyme. With glucose, fucose and galactose the inhibition is competitive. In addition, a transglycosylation mechanism seems to occur. The kinetic studies suggest a substrate-activation model and the presence of two primary active sites: fuco-gluco and galacto.
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PMID:Characterization and kinetics of beta-D-gluco/fuco/galactosidase from sheep liver. 641 26

The activities of various glycosidases in homogenates of the small intestinal mucosa of two adult and 18 suckling tammar wallabies (M. eugenii) aged from 6 to 50 weeks were investigated. Lactase (beta-D-galactosidase), beta-N-acetylglucosaminidase, alpha-L-fucosidase and neuraminidase activities were high during the first 34 weeks post partum and then declined to very low levels. Maltase, isomaltase, sucrase and trehalase activities were very low or absent during the first 34 weeks, and then increased. The lactase activity was unusual in being greater in the distal than the middle or proximal thirds of the intestine, and in its low pH optimum (pH 4.6), inhibition by p-chloromercuribenzene sulfonate but not by Tris, and lack of cellobiase activity. These properties are those of a lysosomal acid beta-galactosidase rather than of a brush border neutral lactase. The maltase activity had the characteristics of a lysosomal acid alpha-glucosidase early in lactation and of a brush border neutral maltase in adult animals. The significance of these findings is discussed in relation to changes in dietary carbohydrates during weaning and to the mode of digestion of milk carbohydrates by the pouch young.
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PMID:Intestinal lactase (beta-galactosidase) and other glycosidase activities in suckling and adult tammar wallabies (Macropus eugenii). 678 21

Bacteroides succinogenes S-85 grows readily in media containing 0.2% (w/v) filter paper cellulose or microcrystalline cellulose as the carbohydrate source. During growth, the cells appear to adhere to the cellulose. Cell-free culture supernates and cell extracts from cellulose-grown cultures had very low hydrolytic activity against either filter paper or crystalline cellulose (Avicel) as substrate, although H3PO4-swollen cellulose, carboxmethylcellulose, and cellobiose were readily hydrolyzed. Cells grown on either cellobiose or glucose exhibited cell-bound carboxymethylcellulase (CMCase) and cellobiase activities. Cultures grown on cellulose had seven to eight times more CMCase activity than either cellobiose- or glucose-grown cultures. Seventy percent of the CMCase activity was present in the supernate, of which 50--60% was associated with sedimentable membranous fragments. the cellobiase, which was largely cell associated, appeared to be constitutive, and the only product detected on enzymic hydrolysis of cellobiose was glucose. The cellobiase activity was strongly inhibited by 0.02 M tris(hydroxymethyl)-aminomethane (Tris), pH 7.1, but this was partially relieved by phosphate ions. These data indicate that B. succinogenes S-85 contains high endo-beta-1,4-glucanase and beta-1,4-glucanase and beta-1,4-glucosidase-like activities.
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PMID:Cellulolytic activity of the rumen bacterium Bacteroides succinogenes. 678 55

Previous studies have shown that Biomphalaria glabrata contains a complete cellulolytic system which includes an endoglucanase, an exoglucanase and a beta-glucosidase. In the present report, a scheme for the purification of the endoglucanase from this invertebrate is proposed. Two major problems were encountered during the study: 1) the presence of a green-brownish pigment, which could not be eliminated by thermal shock or ammonium sulfate precipitation and 2) relative instability of enzymatic activity. Various alternatives were tested and the best sequence of steps was: 1) a sample of the crude extract, obtained by homogenization of the digestive glands in 50 mM Tris-HCl buffer, pH 8.4, and ultracentrifugation, was applied to a Q-Sepharose FPLC column (50 mM Tris-HCl buffer, pH 8.4; 10 mm x 22.2 cm column; flow rate 1.5 ml/min; 0.1 to 0.5 M NaCl gradient); 2) the eluate peak containing activity was dialyzed, lyophilized and eluted from a Superdex-75 gel filtration FPLC column (50 mM ammonium acetate buffer, pH 4.8; 16 mm x 60 cm column; flow rate 1.0 ml/min). A low degree of purification (about 36-fold) and recovery (about 12%) were observed, probably due to enzyme instability. SDS-electrophoresis of the active fraction showed a major peak of 30 kDa. In order to improve the purification scheme, further studies are required to stabilize this enzyme during purification and storage.
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PMID:Partial purification of an endoglucanase from Biomphalaria glabrata. 754 74

From the roots of the Chinese medicinal herb Pseudostellaria heterophylla a single-chained lectin with a molecular weight of 36 kDa and high hemagglutinating activity was isolated. The lectin was adsorbed on DEAE-cellulose in 10 mM Tris-HCI buffer (pH 7.4) and was eluted by the same buffer containing 50 mM NaCl. It was adsorbed on SP-Sepharose in 10mM NH4OAc (pH 4.5) and eluted by approximately 0.5 M NaCl in the same buffer. The hemagglutinating activity of the lectin could not be inhibited by a large variety of monosaccharides, but was largely abrogated by exposure to 0.05 M HCl, 0.05M NaOH or 80 degrees C. However, about 50% of the activity remained after exposure to 0.025M NaOH or 40 degrees C. Despite possession of an N-terminal sequence exhibiting some similarity to thaumatin-like proteins with antifungal activity, the lectin was devoid of antifungal activity. The lectin exerted some inhibitory effect on the glycohydrolases alpha-glucosidase, beta-glucosidase and beta-glucuronidase which are involved in HIV infection but had no suppressive action on human immunodeficiency virus-type 1 reverse transcriptase.
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PMID:A novel lectin from Pseudostellaria heterophylla roots with sequence simularity to Kunitz-type soybean trypsin inhibitor. 1144 23

The hydrolysis of cellulose to the water-soluble products cellobiose and glucose is achieved via synergistic action of cellulolytic proteins. The three types of enzymes involved in this process are endoglucanases, cellobiohydrolases, and beta-glucosidases. One of the best fungal cellulase producers is Trichoderma reesei RUT C30. However, the amount of beta-glucosidases secreted by this fungus is insufficient for effective cellulose conversion. We investigated the production of cellulases and beta-glucosidases in shake-flask cultures by applying three pH-controlling strategies: the pH of the production medium was adjusted to 5.8 after the addition of seed culture with no additional pH adjustment performed, the pH was adjusted to 6.0 daily, and the pH was maintained at 6.0 by the addition of Tris-maleate buffer to the growth medium. Different carbon sources Solka Floc 200, glucose, lactose, and sorbitol were added to standard Mandels nutrients. The lowest beta-glucosidase activities were obtained when no pH adjustment was done regardless of the carbon source employed. Somewhat higher levels of beta- glucosidase were measured in the culture filtrates when daily pH adjustment was carried out. The effect of buffering the culture medium on beta-glucosidase liberation was most prominent when a carbon source inducing the production of other cellulases was applied.
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PMID:beta-Glucosidase production by Trichoderma reesei. 1591 3

Extraction of isoflavone malonylglucosides from red clover (Trifolium pratense L.) is a complicated procedure. This is due to the relatively unstable character of the thermolabile glucoside malonates as well as by action of native beta-glucosidases, resulting in a rapid degradation of malonylated glucosides into their corresponding aglucones. In this study, Tris was identified as a suitable beta-glucosidase inhibitor in red clover extracts, optimized at 350 mM Tris in 80% ethanol at pH 7.2. Extraction of fresh red clover leaves using Tris increased the concentration of malonate conjugated isoflavones approximately 13 to 24 times as opposed to extraction without Tris. A comparison of isoflavone profiles obtained after extraction with and without Tris of different plant organs of red clover and several species within the family Fabaceae suggests that the amount and/or activity of the degenerative beta-glucosidase enzymes vary for the different plant parts of red clover and among the species studied. Therefore, the use of standard extraction methods may well result in overestimation of the concentration of aglucones and consequently underestimation of the malonylglucoside isoflavones concentration depending on the plant species and plant part studied.
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PMID:Extraction of isoflavone malonylglucosides from Trifolium pratense L. 1594 Dec 97


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