| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 69352 | Journal of Molecular Catalysis B: Enzymatic | 2016 | 8 Pages |
•3DOM/m-S was prepared and applied for lipase immobilization.•CALB@3DOM/m-S showed improved stabilities than CALB@3DOM-S.•CALB@3DOM/m-S showed improved usability when applied in esterification.
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.
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