Abstract
Mucor lipase purified was transformed into water-insoluble forms by attaching the enyzme to insoluble carriers covalently and with ionic bond, and some characteristics and kinetics behavior of DEAE-cellulose-lipase were studied in comparing to the soluble form. There was very little difference between the free and bound forms of the lipase with respect to optimum pH, optimum temperature, substrate specificity, action pattern, Km value and the energy of activation, indicating that the immobilization did not alter the substantial properties of the lipase. However, a highly increase in pH and heat stability, a decrease in inhibitory effect of n-bromosuccinimide and iodine, and of the susceptibility towards the action of some proteases were found by the immobilization. The lipolytic activity of the bound lipase was enhanced 4-6 times higher at lower concentration of bile salts, whereas the activity was inhitited at higher concentration. The bound lipase little released from the carrier during lipolysis at 37° for 12-48 hr, although the inactivation caused on it.
