Comparing the effect of immobilization methods on the activity of lipase biocatalysts in ester hydrolysis |
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Authors: | L. Costa V. Brissos F. Lemos F. Ramôa Ribeiro J. M. S. Cabral |
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Affiliation: | IBB-Institute for Biotechnology and Bioengineering, Centre for Biological and Chemical Engineering, Instituto Superior Técnico, Av. Rovisco Pais, 1049-001, Lisboa, Portugal. luis.costa@ist.utl.pt |
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Abstract: | 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. |
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Keywords: | Lipases Zeolite NaY Kinetic modeling Diode array spectrophotometry Spectral deconvolution |
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