Immobilization of lipase from "Fusarium solani" FS1

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