Article ID Journal Published Year Pages File Type
4996678 Bioresource Technology 2018 8 Pages PDF
Abstract

•3DOM/m-OS was prepared using dual templating method for the first time.•CALB was immobilized onto 3DOM/m-OS by adsorption and 'NER' approach.•NER@3DOM/m-OS exhibited excellent stability and reusability.•Alkyl levulinate was synthesized using NER@3DOM/m-OS as biocatalyst.

For conversion of biomass-derived levulinic acid into alkyl levulinates, a novel kind of lipase-based biocatalyst was prepared through immobilized lipase B from C. antarctica (CALB) on organosilica material with highly ordered 3D macroporous organosilica frameworks and a 2D hexagonal meso-structure (named 3DOM/m-OS) for the first time. The catalytic performance of the immobilized lipase (NER@3DOM/m-OS) was investigated. NER@3DOM/m-OS was used as biocatalyst to catalyze the esterification reaction between levulinic acid (LA) and n-butanol. Under optimized reaction conditions, 74.59% of ester yield was achieved after 12 h of reaction. NER@3DOM/m-OS was also used to production of other alkyl levulinates, the ester yields increased to 84.51% (octyl levulinate) and 91.14% (dodecyl levulinate), respectively. When NER@3DOM/m-OS was used repeatedly in batch reactions, the ester yields of n-butyl, octyl, and dodecyl levulinate could retain 46.18%, 82.33% and 81.25% after 9 reaction cycles, respectively, which was better than commercial lipase Novozym 435 under the same condition.

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Physical Sciences and Engineering Chemical Engineering Process Chemistry and Technology
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