Paper Report for: Costa_2008_Bioprocess.Biosyst.Eng_31_323
Reference
Title: Comparing the effect of immobilization methods on the activity of lipase biocatalysts in ester hydrolysis Costa L, Brissos V, Lemos F, Ribeiro FR, Cabral JM Ref: Bioprocess Biosyst Eng, 31:323, 2008 : PubMed
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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Costa L, Brissos V, Lemos F, Ribeiro FR, Cabral JM (2008) Comparing the effect of immobilization methods on the activity of lipase biocatalysts in ester hydrolysis Bioprocess Biosyst Eng31: 323-7
Costa L, Brissos V, Lemos F, Ribeiro FR, Cabral JM (2008) Bioprocess Biosyst Eng31: 323-7