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Biocatalysis and Biotransformation Volume 27, 2009 - Issue 5-6
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Original Article

Improvement of the enantioselectivity and activity of lipase from Pseudomonas sp. via adsorption on a hydrophobic support: kinetic resolution of 2-octanol

Chuang Du Key Laboratory of Molecular Enzymology and Engineering, Ministry of Education, Jilin University, Changchun, People's Republic of China; Changchun Institute of Optics, Fine Mechanics and Physics, Chinese Academy of Sciences, Changchun, People's Republic of China
,
Bo Zhao Key Laboratory of Molecular Enzymology and Engineering, Ministry of Education, Jilin University, Changchun, People's Republic of China
,
Chunyuan Li Key Laboratory of Molecular Enzymology and Engineering, Ministry of Education, Jilin University, Changchun, People's Republic of China
,
Ping Wang Key Laboratory of Molecular Enzymology and Engineering, Ministry of Education, Jilin University, Changchun, People's Republic of China
,
Zhi Wang Key Laboratory of Molecular Enzymology and Engineering, Ministry of Education, Jilin University, Changchun, People's Republic of ChinaCorrespondence[email protected]
,
Jun Tang College of Chemistry, Alan G. MacDiarmid Institute, Jilin University, Changchun, People's Republic of ChinaCorrespondence[email protected]
&
Lei Wang Key Laboratory of Molecular Enzymology and Engineering, Ministry of Education, Jilin University, Changchun, People's Republic of ChinaCorrespondence[email protected]
 show all
Pages 340-347 | Received 11 Apr 2009, Published online: 07 Oct 2009
 
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Abstract

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.

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