1999 Fiscal Year Final Research Report Summary
Elucidation of recognition sites of lipase toward its development as chemical catalysis
| Project/Area Number |
10650859
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Synthetic chemistry
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| Research Institution | Toyama National College of Technology |
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Principal Investigator |
KOMETANI Tadashi Toyama National College of Technology, Department of Chemical and Biochemical Engineering, Professor, 物質工学科, 教授 (60042842)
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| Co-Investigator(Kenkyū-buntansha) |
GOTO Michimasa Toyama National College of Technology, Department of Chemical and Biochemical Engineering, Associate Professor, 物質工学科, 助教授 (70235000)
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| Project Period (FY) |
1998 – 1999
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| Keywords | lipase / hydrolytic activity / enantioselectivity / Candida rugosa |
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| Research Abstract |
The aim of this project is to realize and control an enzymatic reaction as a chemical reaction. The research results are as follows ;
(1) Candida rugosa lipase (CRL) was treated with several concentrations of 2-propanol in water and the changes of the amount of the recovered protein, the hydrolytic activity, and the enentioselectivity toward methyl 2-phenylpropanoate were studied. The results shows that the conformational change of CRL occurred in 30% 2-propanol treatment.
(2) The sizes of the large, medium, and small substituent recognition sites (L, M, and S pocket, respectively) in CRL were roughly estimated by measuring the specific hydrolytic activity against several p-nitrophenyl esters. These relative sizes were assessed as L pocket > phenyl, ethyl > M pocket > methyl > S pocket > hydrogen.
(3) The highly enantioselective transesterification of 2-phenyl-1-propanol, which has not been efficiently resolved by lipase-catalyzed reactions, was attained by using vinyl esters having aromatic ring in acyl moiety as vinyl 3-phenylpropanoate.
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