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Immobilization of lipase from Fusarium solani FS1

Imobilização de lipase de Fusarium solani FS1

Lipase from Fusarium solani FS1 was immobilized by covalent attachment to polyacrylamide beads and onto magnetized Dacron, retaining 12% and 97% of activity, respectively. Lipase was also entrapped within polyacrylamide beads, retaining 53% of activity. Investigations of the kinetic characteristics of the immobilized derivatives using triolein as substrate showed that lipase immobilized onto polyacrilamide beads and Dacron did not follow Michaelis-Menten kinetics.

Fusarium solani FS1; immobilized lipase; enzyme kinetics; Dacron; polyacrylamide beads

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