2000 Fiscal Year Final Research Report Summary
Development of Surfactant Modified Enzymes That Show High Activity in Organic Media.
| Project/Area Number |
10555284
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| Research Category |
Grant-in-Aid for Scientific Research (B).
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| Allocation Type | Single-year Grants |
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| Section | 展開研究 |
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| Research Field |
生物・生体工学
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| Research Institution | KYUSHU UNIVERSITY |
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Principal Investigator |
FURUSAKI Shintaro Faculty of Eng. KYUSHU UNIVERSITY Prof., 大学院・工学研究院, 教授 (40011209)
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| Co-Investigator(Kenkyū-buntansha) |
SEKI Minoru Univ.Tokyo.Faculty of Eng.Assoc.Prof., 大学院・工学系研究院, 助教授 (80206622)
ISHIKAWA Haruo Osaka Fre.Univ.Faculty of Eng.Prof., 大学院・工学研究科, 教授 (00081349)
GOTO Masahiro Faculty of Eng. KYUSHU UNIVERSITY Assoc.Prof., 大学院・工学研究院, 助教授 (10211921)
TSUBOI Hikotada Mitsui Cytec.Co.Ltd., Head of Research, 技術部・部長(研究職)
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| Project Period (FY) |
1998 – 2000
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| Keywords | Surfactant coated enzyme / Organic solvent / Lipase / Protease / Enzyme reaction / Chiral synthesis / Bioengineering / Surfactant |
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| Research Abstract |
The utilization of enzymes in nonaqueous media has been probed to be one of the simplest but the most promising techniques for the enantioselective conversion of various hydrophobic acids and alcohol in the last decade. The high enantioselectivity of enzymes is an attractive feature, in particular, for producing optically active compounds. In our recent investigation, a surfactant-enzyme complex was found to be catalytically active in nonaqueous media. The preparation method of surfactant-enzyme complexes utilizing W/O emulsions is very simple and does not require complicating techniques.
Proteases modified by this preparation method showed high activity in anhydrous organic solvents such as isooctane and toluene. In the present study, a peptide synthesis catalyzed by surfactant-protease complex is conducted in anhydrous organic solvents. The effects of origin of proteases, addition of water, organic solvents, cosolvents were discusses ad well as that of the kind of substrates on the enzymatic activity. The surfactant-protease complexes were thermostable at high temperature, and showed a high storage stability.
The surfactant-lipase complexes were also thermostable at high temperature compared to the native lipase. Furthermore, the lipase complex showed a high storage stability. This modification method will enable us to utilize a lot of enzymes as new biocatalysts which had not shown enzymatic activity in organic media.
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