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Comparing the effect of immobilization methods on the activity of lipase biocatalysts in ester hydrolysis
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Comparing the effect of immobilization methods on the activity of lipase biocatalysts in ester hydrolysis
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Journal Article
Comparing the effect of immobilization methods on the activity of lipase biocatalysts in ester hydrolysis
2008
Overview
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.
Publisher
Springer-Verlag,Springer,Springer Nature B.V
Subject
/ Biological and medical sciences
/ Chemistry and Materials Science
/ Environmental Engineering/Biotechnology
/ Enzymes
/ Enzymes, Immobilized - chemistry
/ Fundamental and applied biological sciences. Psychology
/ Industrial and Production Engineering
/ Industrial Chemistry/Chemical Engineering
/ Kinetics
/ Methods. Procedures. Technologies
/ Zeolites
