title: Comparing the effect of immobilization methods on the activity of lipase biocatalysts in ester hydrolysis.
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.
authors.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
authors.forename: L
authors.initials: L
authors.lastname: Costa
authors.forename: V
authors.initials: V
authors.lastname: Brissos
authors.forename: F
authors.initials: F
authors.lastname: Lemos
authors.forename: F Ramôa
authors.initials: FR
authors.lastname: Ribeiro
authors.forename: J M S
authors.initials: JM
authors.lastname: Cabral
mesh_terms: D002384:Catalysis; D003198:Computer Simulation; D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry*; D004952:Esters / Q000737:chemistry*; D006868:Hydrolysis; D007700:Kinetics; D008049:Lipase / Q000737:chemistry*; D008956:Models, Chemical; D011485:Protein Binding
chemical_list: D004800:Enzymes, Immobilized; D004952:Esters; D008049:Lipase