Purification and characterization of an intracellular beta-glucosidase from Cellulomonas biazotea

beta -Glucosidase from Cellulomonas biazotea NIAB442 was purified by a combination of ammonium sulphate precipitation and ion-exchange chromatography with a 17-fold increase in specific activity. The native and subunit molecular weights of beta -glucosidase were 355 kDa and 92 kDa respectively. The...

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Bibliographic Details
Published in:World journal of microbiology & biotechnology 1997, Vol.13 (2), p.245-247
Main Authors: Siddiqui, K.S, Rashid, M.H, Ghauri, T.M, Durrani, I.S, Rajoka, M.I
Format: Article
Language:English
Subjects:
Biological and medical sciences
Biological Sciences
Biotechnology
Cellulomonas biazotea
Enzyme engineering
Fat industries
Food industries
Fundamental and applied biological sciences. Psychology
Improved methods for extraction and purification of enzymes
Methods. Procedures. Technologies
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Summary:beta -Glucosidase from Cellulomonas biazotea NIAB442 was purified by a combination of ammonium sulphate precipitation and ion-exchange chromatography with a 17-fold increase in specific activity. The native and subunit molecular weights of beta -glucosidase were 355 kDa and 92 kDa respectively. The apparent K sub(m) and V sub(max) values for p-nitrophenyl- beta -D-glucopyranoside (pNPG) were 4.25 mM and 1.526 U /mg protein respectively. The optimum temperature of beta -glucosidase activity was 38 degree C and the pH optimum was 6.6. The thermostability of beta -glucosidase decreased with an increase in pH from 5 to 7. MnCl sub(2) and NaCl inhibited beta -glucosidase activity.
ISSN:0959-3993
1573-0972
DOI:10.1023/A:1018510418900