Crude extracellular invertase from Sclerotium rolfsii, when coupled to glutaraldehyde activated Indion 48-R, retained 70-80% activity of the soluble enzyme. Immobilization resulted in a decrease in the pH and temperature optima but it increased the temperature stability. K-m and V-max also increased as a result of immobilization. Both soluble and immobilized invertase showed inhibition at high substrate concentrations. The bound enzyme showed excellent stability to repeated use and retained approx 90% of its initial activity after 8 cycles of use.