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Improvement of the enantioselectivity and activity of lipase from Pseudomonas sp via adsorption on a hydrophobic support: kinetic resolution of 2-octanol
其他题名论文其他题名
Du C.; Zhao B.; Li C. Y.; Wang P.; Wang Z.; Tang J.; Wang L.
2009
发表期刊Biocatalysis and Biotransformation
ISSN1024-2422
卷号27期号:5—6页码:340-347
摘要Pseudomonas sp. lipase (PSL) was successfully immobilized on a novel hydrophobic polymer support through physical adsorption and the immobilized PSL was used for resolution of (R,S)-2-octanol with vinyl acetate as acyl donor. Enhanced activity and enantioselectivity were observed from the immobilized PSL compared with free PSL. The effects of reaction conditions such as temperature, water activity, substrate molar ratio and the amount of immobilized lipase were investigated. Under optimum conditions, the residual (S)-2-octanol was recovered with 99.5% enantiomeric excess at 52.9% conversion. The results also indicated that the immobilized PSL could maintain 94% of its initial activity even after reusing it five times.
收录类别SCI ; EI
语种英语
文献类型期刊论文
条目标识符http://ir.ciomp.ac.cn/handle/181722/26287
专题中科院长春光机所知识产出
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Du C.,Zhao B.,Li C. Y.,et al. Improvement of the enantioselectivity and activity of lipase from Pseudomonas sp via adsorption on a hydrophobic support: kinetic resolution of 2-octanol[J]. Biocatalysis and Biotransformation,2009,27(5—6):340-347.
APA Du C..,Zhao B..,Li C. Y..,Wang P..,Wang Z..,...&Wang L..(2009).Improvement of the enantioselectivity and activity of lipase from Pseudomonas sp via adsorption on a hydrophobic support: kinetic resolution of 2-octanol.Biocatalysis and Biotransformation,27(5—6),340-347.
MLA Du C.,et al."Improvement of the enantioselectivity and activity of lipase from Pseudomonas sp via adsorption on a hydrophobic support: kinetic resolution of 2-octanol".Biocatalysis and Biotransformation 27.5—6(2009):340-347.
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