Thermostable β-Glucosidase From Thermomonospora Fusca: Purification And Biochemical Characterization

A thermostable β-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. β-Glucosidase was Ju...

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Bibliographic Details
Published in:Journal of applied biological chemistry 2003, 46(1), , pp.6-11
Main Authors: Il Hwan Ryu, Jung Eun Kim, Kap Sang Lee
Format: Article
Language:Korean
Subjects:
characterization
purification
Thermomonospora fusca
β-glucosidase
농학
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Summary:A thermostable β-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. β-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 60℃, respectively. The pH and temperature stability were within a stable ata pH range of 5.0 to 7.5 and at 60℃, respectively. Glucose, the reaction product inhibited β-glucosidase activity. β-Glucosidase was activated by Ca^2+, and inactivated by Fe^2+, Zn^2+, Cu^2+, Ba^2+, Ag^+, Hg^+, iodine, EDTA, and p-CMB. The apparent value of β-glucosidase was 0.76 mM.
ISSN:1976-0442
2234-7941