Simple and efficient immobilization of lipase B from Candida antarctica on porous styrene–divinylbenzene beads

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作者：

K Hernandez，C Garcia-Galan，R Fernandez-Lafuente

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摘要：

Two commercial porous styrene–divinylbenzene beads (Diaion HP20LX and MCI GEL CHP20P) have been evaluated as supports to immobilize lipase B from Candida antarctica (CALB). MCI GEL CHP20P rapidly immobilized the enzyme, permitting a very high loading capacity: around 110 mg CALB/wet g of support compared to the 50 mg obtained using decaoctyl Sepabeads. Although enzyme specificity of the enzyme immobilized on different supports was quite altered by the support used in the immobilization, specific activity of the enzyme immobilized on MCI GEL CHP20P was always higher than those found using decaoctyl Sepabeads for all assayed substrates. Thus, a CALB biocatalyst having 3–8 folds (depending on the substrate) higher activity/wet gram of support than the commercial Novozym 435 was obtained. Half-live of CAL-Diaion HP20LX at 60 °C was 2–3 higher than the one of Novozym 435, it was 30–40 higher in the presence of 50% acetonitrile and it was around 100 folds greater in the presence of 10 M hydrogen peroxide. Results indicate that styrene–divinylbenzene supports may be promising alternatives as supports to immobilize CALB.

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关键词：

Hydrophobic supports Interfacial activation of lipases Lipase features modulation Styrene–divinylbenzene supports Diacetin Hydrogen peroxide

DOI：

10.1016/j.enzmictec.2011.03.002

被引量：

145

年份：

2011