| Purification and Characterization of the Enzyme Cholesterol Oxidase from a New Isolate of Streptomyces sp. | |
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MedLine Citation:
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PMID: 21909628 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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An extracellular cholesterol oxidase (cho) enzyme was isolated from the Streptomyces parvus, a new source and purified 18-fold by ion exchange and gel filtration chromatography. Specific activity of the purified enzyme was found to be 20 U/mg with a 55 kDa molecular mass. The enzyme was stable at pH 7.2 and 50 °C. The enzyme activity was inhibited in the presence of Pb(2+), Ag(2+), Hg(2+), and Zn(2+) and enhanced in the presence of Mn(2+). The enzyme activity was inhibited by the thiol-reducing reagents (DTT, β-mercaptoethanol), suggesting that disulfide linkage is essential for the enzyme activity. The enzyme activity was found to be maximum in the presence of Triton X-100 and X-114 detergents whereas sodium dodecyl sulfate fully inactivated the enzyme. The enzyme showed moderate stability towards all organic solvents except acetone, benzene, chloroform and the activity increased in the presence of isopropanol and ethanol. The K ( m ) value for the oxidation of cholesterol by this enzyme was 0.02 mM. |
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Authors:
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Vandana Praveen; Akanksha Srivastava; C K M Tripathi |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-9-10 |
Journal Detail:
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Title: Applied biochemistry and biotechnology Volume: - ISSN: 1559-0291 ISO Abbreviation: - Publication Date: 2011 Sep |
Date Detail:
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Created Date: 2011-9-12 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8208561 Medline TA: Appl Biochem Biotechnol Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Fermentation Technology Division, Central Drug Research Institute (CSIR), Chattar Manzil, P.O. Box 173, Lucknow, 226 001, Uttar Pradesh, India. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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