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- W2401683831 abstract "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 400 nm and mesopores of 5.1 nm, which provides a promising platform for enzyme immobilization. Lipase B from Candida 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 (288 h). 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." @default.
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- W2401683831 date "2016-08-01" @default.
- W2401683831 modified "2023-10-17" @default.
- W2401683831 title "Immobilization of lipase in hierarchically ordered macroporous/mesoporous silica with improved catalytic performance" @default.
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- W2401683831 doi "https://doi.org/10.1016/j.molcatb.2016.05.009" @default.
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