2014 Fiscal Year Final Research Report
Analysis of catalytic mechanism and activation of a highly stable cholesterol oxidase
| Project/Area Number |
24580127
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Applied microbiology
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| Research Institution | Toyo University |
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Principal Investigator |
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Keywords | コレステロール / コレステロールオキシダーゼ / 臨床検査 |
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| Outline of Final Research Achievements |
High cholesterol levels are strongly associated with cardiovascular disease because these promote atheroma development in arteries. Cholesterol oxidase is useful for enzymatic determination of cholesterol levels in human blood. We previously discovered a thermal, organic solvent and detergent-tolerant cholesterol oxidase from a gram-negative bacterium Chromobacterium sp. DS-1. In addition, it was found that several amino acid residues near the FAD cofactor probably play an important role in the reactivity and the stability of the enzyme. Therefore, we constructed mutant enzymes which had mutated amino acid residues near the FAD cofactor by site directed mutagenesis, to identify amino acid residues that play an important role in activity and stability. In this study, we constructed a mutant enzyme which is relatively stable at high temperature and in the presence of detergents.
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| Free Research Field |
応用微生物学
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