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In relation to this article, we declare that there is no conflict of interest.
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Received May 5, 2013
Accepted October 4, 2013
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 Candida sp.99-125 lipase onto silanized SBA-15 mesoporous materials by physical adsorption

1College of Biotechnology and Pharmaceutical Engineering, Nanjing University of Technology, Nanjing, Jiangsu 210009, China 2Department of Environment and Resource, Nantong Agricultural College, Nantong, Jiangsu 226007, China
hpf@njut.edu.cn
Korean Journal of Chemical Engineering, January 2014, 31(1), 98-103(6), 10.1007/s11814-013-0198-1
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Abstract

SBA-15-NH2 and SBA-15-Cl Mesoporous Materials were prepared by modifying SBA-15 with silane coupling agent 3-aminopropyltriethoxysilane and 3-chloropropyltriethoxysilane using the post-synthesis method. The mesoporous samples were characterized by Fourier transform infrared spectra and nitrogen adsorption. Compared with SBA-15-NH2, SBA-15-Cl has suitable pore opening for further utilization in the immobilization of Candida sp.99-125 lipase by physical adsorption. The influences of lipase concentration and immobilizing time on the immobilization efficiency were investigated. Meanwhile, the lipase immobilized on SBA-15-Cl showed higher thermal, pH and storage stability than that of free lipase. Further study demonstrated that lipase immobilized on SBA-15-Cl could be used eight times without significant decrease of enzyme activity. The phenomenon was associated with the shrinkage of the pore opening of SBA-15-Cl keeping lipase from leaping out.

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