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. 1982 Dec;44(6):1289–1295. doi: 10.1128/aem.44.6.1289-1295.1982

Purification and Properties of β-Glucosidase from Aspergillus terreus

Wesley E Workman 1, Donal F Day 1
PMCID: PMC242187  PMID: 16346147

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 Km values of 0.78 and 0.40 mM for p-nitrophenyl-β-d-glucopyranoside and cellobiose, respectively. Glucose was a competitive inhibitor, with a Ki 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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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