Comparing the effect of immobilization methods on the activity of lipase biocatalysts in ester hydrolysis
Comparing the effect of immobilization methods on the activity of lipase biocatalysts in ester hydrolysis
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DOI：
10.1007/s00449-007-0165-5
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发表时间：
2008-06-01
影响因子：
3.8
通讯作者：
Cabral, J. M. S.
中科院分区：
文献类型：
--
作者：
Costa, L.;Brissos, V.;Cabral, J. M. S.
The activity of various lipases was compared, in both free and immobilized forms, using the kinetics of the hydrolysis reaction of p-nitrophenyl butyrate, which was followed with in situ UV/Vis diode array spectrophotometry. Several enzymes were used to catalyze the reaction, namely Candida antarctica lipase B and Fusarium solani pisi cutinase wildtype and three single-mutation variants. The enzymes were tested in three different forms: free, immobilized as cross-linked aggregates and supported on zeolite NaY. A simple kinetic model was used to allow a quantitative comparison of the behavior of the different catalysts. It was concluded that although immobilization reduces the activity of the enzyme, the zeolite offers a much higher specific activity when compared to the cross-linked aggregates, thus supplying a heterogeneous catalyst with promising catalytic properties.
