Improvement of the enantioselectivity and activity of lipase from Pseudomonas sp via adsorption on a hydrophobic support: kinetic resolution of 2-octanol
Improvement of the enantioselectivity and activity of lipase from Pseudomonas sp via adsorption on a hydrophobic support: kinetic resolution of 2-octanol
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假单胞菌脂肪酶对映选择性和活性的改进。
DOI：
10.3109/10242420903225230
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发表时间：
2009-01-01
影响因子：
1.8
通讯作者：
Wang, Lei
中科院分区：
文献类型：
--
作者：
Du, Chuang;Zhao, Bo;Wang, Lei
采用物理吸附的方法将假单胞菌脂肪酶（PSL）固定在一种新型疏水聚合物载体上，并将固定化后的PSL以乙酸乙烯酯为酰基供体用于（R，S）-2-辛醇的分离。与游离PSL相比，固定化PSL的活性和对映体选择性增强。考察了反应温度、水活度、底物摩尔比、固定化脂肪酶用量等条件对反应的影响。在最佳条件下，残余(S)-2-辛醇的回收率为99.5%，对映体残留量为52.9%。结果还表明，即使重复使用5次，固定化PSL仍能保持其初始活性的94%。
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.