|کد مقاله||کد نشریه||سال انتشار||مقاله انگلیسی||ترجمه فارسی||نسخه تمام متن|
|4996678||1368272||2018||8 صفحه PDF||سفارش دهید||دانلود کنید|
- 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 12Â 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.
Journal: Bioresource Technology - Volume 247, January 2018, Pages 568-575