Bhattacharjee, B. ; Roy, A. ; Majumder, A. L. (1992) β-Glucosidase of a white-rot fungus Trametes gibbosa Biochemistry International, 28 (5). pp. 783-793. ISSN 0158-5231
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Abstract
Extracellular beta-glucosidase was purified from a white-rot fungus, Trametes gibbosa by 50% ammonium sulphate saturation and Sephadex G-100 column chromatography. It showed maximum activity towards p-nitrophenyl- beta-D- glucopyranoside (pNpG). The pH optimum was 3.5. Temperature optimum was 40 degrees C but shifted to 50 degrees C on preincubation with pNpG. Hg2+, Fe3+ and Cu2+ strongly inhibited the activity. The enzyme was competitively inhibited by glucose with a Ki of 5.2 mM. The apparent molecular mass as determined by gel filtration chromatography was 640 kDa.
Item Type: | Article |
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Source: | Copyright of this article belongs to International Union of Biochemistry. |
ID Code: | 86108 |
Deposited On: | 12 Mar 2012 13:43 |
Last Modified: | 12 Mar 2012 13:43 |
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