PREPARATION AND PROPERTIES OF SCLEROTIUM-ROLFSII INVERTASE IMMOBILIZED ON INDION 48-R

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 t emperature optima but it increased the temperature stability. K-m and V-max also increased as a result of immobilization. Both soluble and i mmobilized invertase showed inhibition at high substrate concentration s. The bound enzyme showed excellent stability to repeated use and ret ained approx 90% of its initial activity after 8 cycles of use.