1992 Fiscal Year Final Research Report Summary
Development of superbioreactors
| Project/Area Number |
03555179
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| Research Category |
Grant-in-Aid for Developmental Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
有機工業化学
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| Research Institution | Kyushu Institute of Technology |
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Principal Investigator |
KONDO Hiroki Department of Biochemical Engineering and Science, Kyushu Institute of Technology, professor, 情報工学部, 教授 (60038057)
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| Co-Investigator(Kenkyū-buntansha) |
KURASHIGE Jun Ajinomoto Corp.,vice manager, 中央研究所油脂研究所, 副部長
SONOMOTO Kenji Department of Biochemical Engineering and Science, associate professor, 情報工学部, 助教授 (10154717)
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| Project Period (FY) |
1991 – 1992
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| Keywords | organic solvent systems / chemical modification of enzymes / lipases / conversion of enzyme functions / organic silicon compounds / stereoselective esterification / support-free bioreactors / tubular |
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| Research Abstract |
A.Development of catalytic devices (1)Conversion of enzyme functions by chemical modification: Upon chemical modification of tyrosine residues of a Pseudomonaslipase, its esterase activity was reduced drastically, while lipase activity was little affected. This phenomenon was observed when two of the tyrosine residues of this enzyme were modified. (2) Search of biocatalysts effective for transformation of unnatural compounds: Enzymatic optical resolution of 2-trimethylsily(TMS)-1- propanol(A),1-TMS-2-propanol(B) and 1-TMS-1-propanol(C) was attempted. Unlike chemical methods, enzymatic methods were found to be superior for esterifying A and B with 5-phenylvaleric acid. Furthermore, efficient optical resolution was achieved for B with Pseudomonas sp. lipoprotein lipase. Because of a steric bulk, C reacted more slowly than A and B. but a significant stereoselectivity was observed for C as well.
B.Development of support-free biocatalyst
Stereoselective esterification of dl-2-(4-chlorophenoxy) propionic acid with myristyl alcohol was carried out in water-saturated carbon tetrachloride-issoctanol (8:2) in the presence of yeast lipase OF360 at 30ﾟC. A 3-fold higher rate and high stereoselectivity was observed for enzyme powder than that for celite-adsorbed enzyme. As an application a continuous reactor was developed in which a glass column was filled with enzyme powder. This system yielded a 4-fold higher productivity than the celite-adsorbed enzyme.
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