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Beta-glucosidase of a white-rot fungus Trametes gibbosa.

Authors
  • Bhattacharjee, B
  • Roy, A
  • Majumder, A L
Type
Published Article
Journal
Biochemistry international
Publication Date
Dec 01, 1992
Volume
28
Issue
5
Pages
783–793
Identifiers
PMID: 1288491
Source
Medline
License
Unknown

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.

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