Immobilization of lipase in hierarchically ordered macroporous/mesoporous silica with improved catalytic performance

Publication date: Available online 19 May 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Yanjun Jiang, Pengju Zheng, Liya Zhou, Weixi Kong, Jing Gao, Jinxia Wang, Jinyan Gu, Xu Zhang, Xiaomei Wang Hierarchically ordered macroporous/mesoporous silica (3DOM/m-S) material was prepared through the dual templating method with polystyrene (PS) colloidal crystals as the hard template and amphiphilic triblock copolymers (P123) as the soft template. The achieved 3DOM/m-S possesses ordered macropores of 400nm and mesopores of 5.1nm, which provides a promising platform for enzyme immobilization. Lipase B from C. antarctica (CALB) was employed as a model enzyme to verify the possibility and advantages of enzyme immobilized on 3DOM/m-S. The immobilized lipase shows excellent stability towards heat even at 80°C and organic solvents for long-term incubation (288h). Also, the immobilized CALB could be used for esterification reactions between acids and alcohols with different chain lengths, and 90% of conversion rate could be reached. In examining the reusability in esterification of oleic acid and ethanol, the conversion rate can retain 75% after 10 reaction cycles, indicating a remarkable reusability of the immobilized lipase. Graphical abstract

Source: Journal of Molecular Catalysis B: Enzymatic - May 19, 2016 Category: Biochemistry Source Type: research