Recombinant cutinase from Fusarium solani pisi was covalently attached to dextran and two derivatized silica supports, Biosil-NH2 and Biosil-Dextran-NH2. Kinetic parameters were determined for all three systems as well as for soluble cutinase. Long-term stability in aqueous media was studied; dextran may have a stabilizing role not only die to the covalent links involved but also in the same way as other polyhydroxides in aqueous media. Differential scanning calorimetry analysis suggests an enhancement of conformational stability of the immobilized forms.