IMMOBILIZATION STABILIZATION ON DIFFERENT HYDROXYLIC SUPPORTS OF LIPASE FROM CANDIDA-RUGOSA

Lipase from Candida rugosa has been covalently immobilized on tosyl activated matrix (agarose and corn cob) and optimum immobilisation conditions determined. The immobilized derivatives exhibited greater residual activity than the ones reported previously. Studies on the activity and stability of the different insolubilized derivatives prepared showed that the enzymatic derivative immobilized on small corn cob is resistant to inactivation by temperature, at 50-degrees-C. This derivative was 100 times more stable than its soluble counterpart. The insolubilized derivatives are more active and stable at higher temperatures (> 35-degrees-C) than soluble enzyme. Lipase activity (using olive oil emulsion) and esterase activity (using p-nitrophenyl butyrate) have been determined. Kinetic studies have been carried out with soluble and immobilized derivatives. The influence of Na (I) and Ca (II) on the lipase and esterase activities is discussed.