Document Detail

Purification and characterization of beta-glucosidase from Bacteroides JY-6, a human intestinal bacterium.
MedLine Citation:
PMID:  8889027     Owner:  NLM     Status:  MEDLINE    
A beta-glucosidase (EC was purified 2500-fold from Bacteroides JY-6, an intestinal anaerobic bacterium of human. The specific activity of the homogeneously purified enzyme was 210 mumol/min/mg protein. The enzyme (M(r) 75kDa) was an monomer whose pI and optimal pH values were 4.6 and 5.5-6, respectively. The best substrates were p-nitrophenyl beta-D-glucopyranoside and natural beta-bound glucosides, such as prunin and poncirenin. Puerarin, which is a C-glycoside, was weakly effective. However, cellobiose, alpha-bound glycosides and rhamnoglucosides were not effective. The apparent Kms for prunin and p-nitrophenyl-beta-D-glucopyranoside were determined to be 0.08 and 0.19 mM, respectively. The enzyme was strongly inhibited by p-chloromercuriphenylsulfonic acid and reaction products such as p-nitrophenol and glucose.
D H Kim; I S Sohng; K Kobashi; M J Han
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biological & pharmaceutical bulletin     Volume:  19     ISSN:  0918-6158     ISO Abbreviation:  Biol. Pharm. Bull.     Publication Date:  1996 Sep 
Date Detail:
Created Date:  1997-02-24     Completed Date:  1997-02-24     Revised Date:  2004-11-17    
Medline Journal Info:
Nlm Unique ID:  9311984     Medline TA:  Biol Pharm Bull     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  1121-5     Citation Subset:  IM    
College of Pharmacy, Kyung-Hee University, Seoul, Korea.
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MeSH Terms
Bacterial Proteins / analysis
Bacteroides / enzymology*
Electrophoresis, Polyacrylamide Gel
Feces / microbiology
Hydrogen-Ion Concentration
Intestines / microbiology*
Molecular Weight
Spectrophotometry, Ultraviolet
Substrate Specificity
beta-Glucosidase / analysis*,  isolation & purification,  metabolism
Reg. No./Substance:
0/Bacterial Proteins; EC

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