| Stabilization of Aspergillus parasiticus cytosine deaminase by immobilization on calcium alginate beads improved enzyme operational stability. | |
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MedLine Citation:
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PMID: 23030840 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Cytosine deaminase (CD) from Aspergillus parasiticus, which has half-life of 1.10 h at 37°C, was stabilized by immobilization on calcium alginate beads. The immobilized CD had pH and temperature optimum of 5 and 50°C respectively. The immobilized enzyme also stoichiometrically deaminated Cytosine and 5-fluorocytosine (5-FC) with the apparent K(M) values of 0.60 mM and 0.65 mM respectively, displaying activation energy of 10.72 KJ/mol. The immobilization of native CD on calcium alginate beads gave the highest yield of apparent enzymatic activity of 51.60% of the original activity and the enzymatic activity was lost exponentially at 37°C over 12 h with a half-life of 5.80 h. Hence, the operational stability of native CD can be improved by immobilization on calcium alginate beads. |
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Authors:
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H Zanna; A J Nok; S Ibrahim; H M Inuwa |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-10-3 |
Journal Detail:
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Title: Journal of enzyme inhibition and medicinal chemistry Volume: - ISSN: 1475-6374 ISO Abbreviation: J Enzyme Inhib Med Chem Publication Date: 2012 Oct |
Date Detail:
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Created Date: 2012-10-3 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101150203 Medline TA: J Enzyme Inhib Med Chem Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Department of Biochemistry, Faculty of Science, University of Maiduguri , Maiduguri , Nigeria. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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