Purification and characterization of beta-1,4-glucosidase from Clostridium papyrosolvens.

Sharmila, T and Sreeramulu, G and Nand, K (1998) Purification and characterization of beta-1,4-glucosidase from Clostridium papyrosolvens. Biotechnology and Applied Biochemistry, 27. pp. 175-9. ISSN 0885-4513

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Abstract

Clostridium papyrosolvens CFR-1010 was selected for the anaerobic extracellular production of beta-1,4-glucosidase. The enzyme was purified by alcohol precipitation and DEAE ion-exchange chromatography. Its homogeneity was confirmed by SDS/PAGE. The enzyme had a molecular mass of 85 kDa. The maximum enzyme activity was observed at pH 5.0 and 50 degrees C. The enzyme activity was inhibited by Ca2+, Co2+, Cu2+, Zn2+, Fe2+, Mg2+ and Na+ ions. However, the activity increased (158%) in the presence of MnCl2, whereas it decreased by 80% in the presence of N-bromosuccinimide, suggesting the presence of tryptophan residues at the active site of enzyme. The enzyme had a K(m) of 15 mg/ml and Vmax of 125 units/min per mg of protein.

Item Type:	Article
Uncontrolled Keywords:	clostridium papyrosolvens, beta glucosidase, purification
Subjects:	500 Natural Sciences and Mathematics > 07 Life Sciences > 04 Microbiology > 02 Bacteriology
Divisions:	Food Microbiology
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	12 Nov 2021 10:42
Last Modified:	12 Nov 2021 10:42
URI:	http://ir.cftri.res.in/id/eprint/2207

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