Document Detail

Characterization and chillproofing activity of two enzymes from Streptomyces species.
MedLine Citation:
PMID:  8676279     Owner:  NLM     Status:  MEDLINE    
Two enzymes, amylase and protease of Streptomyces species were purified by a combination of ion exchange chromatography and gel filtration and characterized. The amylase had an exoaction on starch yielding maltose as a major end product and was identified as beta-amylase. The purified amylase had a molecular weight of 48,000 and was maximally active at 35 degrees C and at pH 6.0. On the other hand, protease had a molecular weight of 21,000 and was most active at pH 10.0 and at a temperature of 30 degrees C. The Km or MICHAELIS constant of amylase for maize starch was 0.333 mg/ml while that of protease for casein was 2.5 mg/ml. The feasibility of using the purified protease for various industrial application especially in the chillproofing of beer is discussed.
C A Etok; O U Eka
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of basic microbiology     Volume:  36     ISSN:  0233-111X     ISO Abbreviation:  J. Basic Microbiol.     Publication Date:  1996  
Date Detail:
Created Date:  1996-08-12     Completed Date:  1996-08-12     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8503885     Medline TA:  J Basic Microbiol     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  83-8     Citation Subset:  IM    
Department of Biological Sciences, University of Calabar, Nigeria.
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MeSH Terms
Endopeptidases / chemistry,  isolation & purification,  metabolism*
Hydrogen-Ion Concentration
Industrial Microbiology
Molecular Weight
Streptomyces / enzymology*
beta-Amylase / chemistry,  isolation & purification,  metabolism*
Reg. No./Substance:
EC; EC 3.4.-/Endopeptidases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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