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Appl Environ Microbiol. 1982 December; 44(6): 1289-1295
Copyright © 1982, American Society for Microbiology. All Rights Reserved.

Purification and Properties of ß-Glucosidase from Aspergillus terreus

Wesley E. Workman and Donal F. Day

1 Department of Microbiology and Audubon Sugar Institute, 2 Louisiana State University, Baton Rouge, Louisiana 70803

ABSTRACT

A ß-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 ß-glucosidase had Km values of 0.78 and 0.40 mM for p-nitrophenyl-ß-D-glucopyranoside and cellobiose, respectively. Glucose was a competitive inhibitor, with a Ki of 3.5 mM when p-nitrophenyl-ß-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-ß-D-glucopyranoside and cellobiose substrates, respectively. Cations, proteases, and enzyme inhibitors had little or no effect on the enzyme activity. The ß-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 ß-glucosidase exhibited for cellobiose compared favorably with the values obtained for ß-glucosidases from other organisms being studied for use in industrial cellulose saccharification.

Appl Environ Microbiol. 1982 December; 44(6): 1289-1295
Copyright © 1982, American Society for Microbiology. All Rights Reserved.





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Copyright © 1982 by the American Society for Microbiology. All rights reserved.