Lipase from Fusarium solani FSl was immobilized by covalent attachment to p
olyacrylamide beads and onto magnetized Dacron, retaining 12% and 97% of ac
tivity, 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 lipa
se immobilized onto polyacrilamide beads and Dacron did not follow Michaeli
s-Menten kinetics.