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• W1528260369 startingPage "1289" @default.
• W1528260369 abstract "A β-glucosidase (EC 3.2.1.21) from the fungus Aspergillus terreus was purified to homogeneity as indicated by disc acrylamide gel electrophoresis. Optimal activity was observed at pH 4.8 and 50°C. The β-glucosidase had K m values of 0.78 and 0.40 mM for p -nitrophenyl-β- d -glucopyranoside and cellobiose, respectively. Glucose was a competitive inhibitor, with a K i of 3.5 mM when p -nitrophenyl-β- d -glucopyranoside was used as the substrate. The specific activity of the enzyme was found to be 210 IU and 215 U per mg of protein on p -nitrophenyl-β- d -glucopyranoside and cellobiose substrates, respectively. Cations, proteases, and enzyme inhibitors had little or no effect on the enzyme activity. The β-glucosidase was found to be a glycoprotein containing 65% carbohydrate by weight. It had a Stokes radius of 5.9 nm and an approximate molecular weight of 275,000. The affinity and specific activity that the isolated β-glucosidase exhibited for cellobiose compared favorably with the values obtained for β-glucosidases from other organisms being studied for use in industrial cellulose saccharification." @default.
• W1528260369 created "2016-06-24" @default.
• W1528260369 creator A5016377795 @default.
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• W1528260369 date "1982-12-01" @default.
• W1528260369 modified "2023-09-26" @default.
• W1528260369 title "Purification and Properties of β-Glucosidase from <i>Aspergillus terreus</i>" @default.
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• W1528260369 doi "https://doi.org/10.1128/aem.44.6.1289-1295.1982" @default.
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