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 cellulolytic actinomycete Streptomyces sp. QM-B814 possess an intracellular beta-glucosidase system which is induced by cellobiose and carboxymethylcellulose. Maximal beta-glucosidase activity was attained 8-10 h after inducer addition to exponential phase growing cultures. The induction is depressed in the presence of glucose. The system is composed of two electrophoretically different beta-glucosidases forms showing relative molecular masses of about 60 and 35 kDa, and pI values in the range 4.2-4.5. Both beta-glucosidases are synthesized de novo. The enzymes share substrate preference and are both inhibited by delta-gluconolactone and p-chloromercuribenzoate. The induction pattern and glucose inhibition are similar for both enzymes.
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PMID:Induction and preliminary characterization of intracellular beta-glucosidases from a cellulolytic Streptomyces strain. 778 69

The reported polyacrylamide gel electrophoresis banding pattern for the main beta-glucosidase (linamarase) component from flax seed consists of five bands, made up of 62.5 and 65 kDa subunits; this component has an estimated molecular weight of 570-670 kDa. The present study used Ferguson plots to estimate the molecular weight of each electrophoretic band, plus two additional bands which were detected. From low to high relative mobility, the seven bands formed a linear series with estimated molecular weights from 1200 to 245 kDa. Each was 160 kDa smaller, and less charged, than the preceding band. This 160 kDa difference between bands did not appear to be consistent with the reported subunit size. Each band produced a corresponding band on sodium dodecyl sulfate (SDS)-gels. The decreases in molecular weight between the bands on nondenaturing gels and their corresponding bands on SDS-gels were multiples of the 62-65 kDa value. However, the estimated molecular weights of the SDS bands themselves and of the differences between the SDS bands were, again, not consistent with the proposed subunit size. The results suggest that active forms of this enzyme may contain a second minor component (possibly a 30-35 kDa component) in addition to the 62.5 and 65 kDa subunits.
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PMID:An examination of the beta-glucosidase (linamarase) banding pattern in flax seedlings using Ferguson plots and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. 792 45

The thermotolerant Aspergillus niveus strain RMF 7883 was grown in Czapek medium, with filter paper cellulose. The proportion of mycelial-bound to extracellular enzymes was studied. Most of the beta-glucosidase (80.9%) and endoglucanases (78.3%) activities were extracellular. The extracellular endoglucanases and beta-glucosidase were separated and partially purified by Sephadex G-100 gel filtration, followed by ion exchange chromatography on CM-trisacryl M. Two extracellular endoglucanases, EG I and EG II (130 kDa and 35 kDa, respectively), and beta-glucosidase (194 kDa) were isolated from culture filtrate.
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PMID:Separation and partial purification of beta-glucosidase and two endoglucanases in Aspergillus niveus. 901 40

Extracellular enzymes from Lentinus edodes M290 on normal woods (Quercus mongolica) and waste logs from oak mushroom production were comparatively investigated. Endoglucanase, cellobiohydrolase, beta-glucosidase, and xylanase activities were higher on waste mushroom logs than on normal woods after L. edodes M290 inoculation. Xylanase activity was especially different, with a three times higher activity on waste mushroom logs. When the waste mushroom logs were used as a carbon source, a new 35 kDa protein appeared. After the purification, the optimal pH and temperature for xylanase activity were determined to be 4.0 and 50 degrees C, respectively. More than 50% of the optimal xylanase activity was retained when the temperature was increased from 20 to 60 degrees C, after a 240 min reaction. At 40 degrees C, the xylanase maintained 93% of the optimal activity, after a 240 min reaction. The purified xylanase showed a very high homology to the xylanase family 10 from Aspergillus terreus by LC/MS-MS analysis. The highest Xcorr (1.737) was obtained from the peptide KWI SQGIPIDGIG SQTHLGSGGS WTVK originated from Aspergillus terreus, indicating that the 35 kDa protein was xylanase. This protein showed low homology to a previously reported L. edodes xylanase sequence.
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PMID:Characterization of xylanase from Lentinus edodes M290 cultured on waste mushroom logs. 1809 65