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Thermostable beta-glucosidase from Thermomonospora fusca: Purification and biochemical characterization

Thermostable beta-glucosidase from Thermomonospora fusca: Purification and biochemical characterization

Agricultural Chemistry & Biotechnology 46(1): 6-11, March

A thermostable beta-glucosidase obtained from a strain of thermophillic actinomyces Thermomonospora fusca (ATCC 27730) was successively purified by ethanol precipitation, ion exchange chromatography, and gel-filtration chromatography with an overall purification of about 4.39-fold. beta-Glucosidase was judged as a single protein band by polyacrylamide gel electrophoresis, and its molecular weight was determined to be 45,000 by SDS-polyacrylamide gel electrophoresis and gel-filteration column chromatography. Optimal pH and temperature for the enzyme activity were 6.5 and 60degreeC, respectively. The pH and temperature stability were within a stable at a pH range of 5.0 to 7.5 and at 60degreeC, respectively. Glucose, the reaction product inhibited beta-glucosidase activity. beta-Glucosidase was activated by Ca2+ and Mn2+, and inactivated by Fe2+, Zn2+, Cu2+, Ba2+, Ag+, Hg+, iodine, EDTA, and p-CMB. The apparent value of beta-glucosidase was 0.76 mM.

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Accession: 011564036

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