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)

Affinity chromatography of a commercial preparation of beta-glucosidase from Aspergillus niger using concanavalin A-Sepharose (CAS) was employed as a means of purifying this glycoprotein. However, mannose (up to 1.08 M) was ineffective as an eluent of this enzyme from CAS, as were several other sugars and their derivatives, including 0.5 M glucose. Also, washing the CAS: beta-glucosidase complex with buffer at pH 3.5 in the absence of MnCl2 and CaCl2 (required to preserve the binding activity of concanavalin A below pH 5.0) did not result in elution of this enzyme. On the contrary, endoglucanase activity present in a crude cellulase complex (A. niger) which bound to CAS could be eluted by mannose (0.5-0.7 M) and was fractionated into at least two components. The CAS: beta-glucosidase complex hydrolyzed cellobiose to glucose and possessed an activity of 2,158 units/g dry CAS. It could be used, therefore, for continuous cellobiose hydrolysis without leakage of enzyme from the support.
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PMID:Affinity chromatography of beta-glucosidase and endo-beta-glucanase from Aspergillus niger on concanavalin A-Sepharose: implications for cellulase component purification and immobilization. 310 Oct 58

Oat beta-glucosidase (EC 3.2.1.21) has two isomeric forms, type I and type II, which are composed of 60 kDa peptides. To study the subunit composition and the stability of multimeric structure, the type I and II were purified from the primary leaves and coleoptiles of the etiolated oat seedlings where the isozymes are expressed organ-specifically. The monomers of the isozymes were isolated by urea-denatured gel electrophoresis followed by electroblotting. N-Terminal amino acid sequencing of the monomers indicated that the type I consisted of a peptide of ALESAKQVKPWQVPKRDWFP (As-Glu 1), and the type II having a peptide of ALESGKLKPWQIPKRDWFP (As-Glu 2) and As-Glu 1 in 1:1 ratio. The C-terminal amino acid of the As-Glu 1 was alanine and that of the As-Glu 2 was lysine. The As-Glu 2 was more negatively charged than the As-Glu 1. The type I isozyme is thus homomultimer of As-Glu 1 monomer and the type II heteromultimer of As-Glu 1 and As-Glu 2 monomers in 1:1 ratio. Partial denaturation of the multimers with urea and CaCl2 broke down the higher multimers to the lower multimers, which were in turn dissociated into homodimers and heterodimer. Denaturation study with urea and CaCl2 indicate that the higher multimers of the homooligomeric type I were more stable than those of the heterooligomeric type II and that hydrophobic interactions were important in the multimer formation. The homodimers were found to be more stable than the heterodimer. These results indicate that different combinations of the As-Glu 1 and As-Glu 2 monomers form the two isozymes of oat beta-glucosidase with different enzymatic properties and structural stability.
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PMID:Subunit composition and oligomer stability of oat beta-glucosidase isozymes. 985 80

Beta-D-Glucopyranosidase (betaG, EC 3.2.1.21) has been isolated from some collateral activities, alpha-L-arabinofuranosidase (Ara, EC 3.2.1.55), alpha-L-rhamnopyranosidase (Rha, EC 3.2.1.40), and o-acetylesterase (Est, EC 3.1.1.53), using a commercial enzyme preparation and a simple method economically sustainable for the food industry. The procedure comprises precipitation of extraneous substances by adding ethanol and CaCl2, ultrafiltration, and adsorption, first on bentonite and then on chitosan. The results obtained were the complete isolation of betaG from the above-mentioned activities, a drastic reduction in extraneous compounds, such as brown substances and polysaccharides, and a slight increase in purification.
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PMID:Inexpensive isolation of beta-D-glucopyranosidase from alpha-L-arabinofuranosidase, alpha-L-rhamnopyranosidase, and o-acetylesterase. 1200 63

Cellulase production by the fungi Trichoderma reesei was studied using dairy manure as a substrate. Data showed that T. reesei RUT-C30 had higher cellulase production than T. reesei QM 9414 and that a homogenized manure, treated by a blender to reduce fiber size, led to higher cellulase production. The cellulase production was further optimized by growing T. reesei RUT-C30 on homogenized manure. The effects of manure concentration, pH, and temperature on cellulase production were investigated with optimal parameter values determined to be 10 g/l manure (dry basis), 25.5 degrees C, and pH 5.7, respectively. Elimination of CaCl2, MgSO4, nitrogen sources (NH4+ and urea) and trace elements (Fe2+, Zn2+, Co2+ and Mn2+) from the original salt solution had no negative influence on the cellulase production, while phosphate elimination did reduce cellulase production. Based on above results, the final medium composition was simplified with manure additives being KH2PO4, tween-80 and CoCl2 only. Using this medium composition and a reaction time of 6-8 days, a maximum cellulase production activity of 1.74 IU/ml of filter paper activity, 12.22 IU/ml of CMCase activity, and 0.0978 IU/ml of beta-glucosidase was obtained. This filter paper activity is the highest ever reported in cellulase production from agricultural wastes.
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PMID:Production of cellulase by Trichoderma reesei from dairy manure. 1549 32

Protoplasts of Aspergillus oryzae 3.481 and Aspergillus niger 3.316 were prepared using cellulose and snail enzyme with 0.6 M NaCl as osmotic stabilizer. Protoplast fusion has been performed using 35% polyethylene glycol 4.000 with 0.01 mM CaCl2. The fused protoplasts have been regenerated on regeneration medium and fusants were selected for further studies. An intracellular beta-glucosidase (EC 3.2.1.21) was purified from the protoplast fusant of Aspergillus oryzae 3.481 and Aspergillus niger 3.316 and characterized. The enzyme was purified 138.85-fold by ammonium sulphate precipitation, DE-22 ion exchange and Sephadex G-150 gel filtration chromatography with a specific activity of 297.14 U/mg of protein. The molecular mass of the purified enzyme was determined to be about 125 kDa by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The enzyme had an optimum pH of 5.4 and temperature of 65 degrees C, respectively. This enzyme showed relatively high stability against pH and temperature and was stable in the pH range of 3.0-6.6. Na+, K+, Ca2+, Mg2+ and EDTA completely inhibited the enzyme activity at a concentration of 10 mM. The enzyme activity was accelerated by Fe3+. The enzyme activity was strongly inhibited by glucose, the end product ofglucoside hydrolysis. The K(m) and V(max) values against salicin as substrate were 0.035 mM and 1.7215 micromol min(-1), respectively.
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PMID:Purification and characterization of an intracellular beta-glucosidase from the protoplast fusant of Aspergillus oryzae and Aspergillus niger. 2125 29