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- W809294359 abstract "A thermostable -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. -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 , respectively. The pH and temperature stability were within a stable at a pH range of 5.0 to 7.5 and at , respectively. Glucose, the reaction product inhibited -glucosidase activity. -Glucosidase was activated by and , and inactivated by , , , , , , iodine, EDTA, and p-CMB. The apparent value of -glucosidase was 0.76 mM." @default.
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- W809294359 date "2003-01-01" @default.
- W809294359 modified "2023-09-28" @default.
- W809294359 title "Thermostable ${beta}$-Glucosidase from Thermomonospora fusca: Purification and Biochemical Characterization" @default.
- W809294359 hasPublicationYear "2003" @default.
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