Lipase immobilized in ordered mesoporous silica: A powerful biocatalyst for ultrafast kinetic resolution of racemic secondary alcohols

文献类型： 外文期刊

第一作者： Zheng, Mingming

作者： Zheng, Mingming;Xiang, Xia;Wang, Shi;Shi, Jie;Deng, Qianchun;Huang, Fenghong;Deng, Qianchun;Cong, Renhuai;Deng, Qianchun;Cong, Renhuai

作者机构：

关键词： Lipase;Ordered mesoporous silica;Biocatalyst;Kinetic resolution;Secondary alcohols

期刊名称：PROCESS BIOCHEMISTRY （ 影响因子：3.757； 五年影响因子：3.665 ）

ISSN： 1359-5113

年卷期： 2017 年 53 卷

页码：

收录情况： SCI

摘要： Although Burkholderia cepacia lipase (BCL) has been proved to be a potential catalyst for chiral resolution, it is rarely applied in industry because of the low catalysis activity and poor stability of the free form. In this article, BCL was immobilized on the phenyl-modified ordered mesoporous silica (Ph-OMMs) to obtain a novel immobilized lipase. Benefits from the bottle-neck mesoporous structure, high loading of BCL could be completed within only 15 min. When BCL@Ph-OMMs was used as a catalyst for the resolution of 1-phenylethanol, up to 50% conversion with more than 99% ee(s) was obtained within only 25 min, which is about 65-folds faster than that of the free lipase. Stabilized BCL@Ph-OMMs was successfully used for the ultrafast resolution of six secondary alcohols by selectivity transesterification, which reached high conversion (50%) and high enantioselectivity (>= 99%) within 20-180 min. The activity of BCL@Ph-OMMs was kept relatively constant in 50 consecutive cycles, which is the best result among the reported immobilized lipases. The study suggests that BCL@Ph-OMMs is an attractive catalyst in industrial applications. (C) 2016 Elsevier Ltd. All rights reserved.

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