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In relation to this article, we declare that there is no conflict of interest.
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Received October 11, 2014
Accepted December 26, 2014
articles This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Immobilization of lipase onto aminopropyl-functionalized MSU-H type mesoporous silica and esterification

Zhijiang College, Zhejiang University of Technology, Hangzhou 310024, P. R. China 1Research Group for Advanced Materials & Sustainable Catalysis (AMSC), College of Chemical Engineering, Zhejiang University of Technology, Hangzhou 310014, P. R. China 2College of Biological and Environmental Engineering, Zhejiang University of Technology, Hangzhou 310014, P. R. China
Korean Journal of Chemical Engineering, August 2015, 32(8), 1694-1700(7), 10.1007/s11814-014-0391-x
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Abstract

Candida rugosa lipase (CRL) was immobilized on an aminopropyl-functionalized MSU-H type mesoporous silica (AFMS) through physical adsorption and a covalent cross-linking. It was evaluated as a class of biocatalysts in the esterification of conjugated linoleic acid (CLA) isomers with ethanol. AFMS materials with varied content of aminopropyl were prepared by a simple co-condensation at near neutral pH condition. Introduction of aminopropyl chains and CRL molecules onto the AFMS supports was confirmed by Fourier transform infrared (FT-IR) spectra. CRL was immobilized on the AFMS through electrostatic and covalent interactions. The covalently cross-linked CRL gave a loading amount of 34.3mg CRL/g-support and a hydrolytic activity of 2471.5U/g-catalyst. It exhibited high operational stability and remained 23.9-27.5% of total esterification in 32 h consecutive four runs in the esterification of CLA with ethanol. Moreover, the immobilized CRLs catalyzed 2.8-3.8 times of esterification of cis-(c)9, trans-(t)11-CLA faster than that of t10, c12-CLA.

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