A Yasinian

Candida rugosa lipase (Type VI-B) from porcine pancreas was immobilized on cloisite (30B) membrane which is activated with epichlorohydrin. The membrane was characterized using SEM, FTIR and contact angle techniques. The effect of different parameters such as enzyme concentration, pH, temperature, magnetic stirring, concentration of substrate and incubation time on enzyme activity were evaluated. Moreover, reusability and kinetic behavior of covalent immobilized lipase were studied. The retained activity of the immobilized lipase was higher than free enzyme. Kinetic analysis shows that the dependence of lipolytic activity of both free and immobilized lipase on substrate concentration can be described by Michaelis–Menten model

Candida rugosa lipase, Enzyme Immobilization, Epichlorohydrin (ECH)