LIPASE IMMOBILIZED ON HYDROPHOBIC MICROPOROUS POLYPROPYLENE FOR THE HYDROLYSIS OF PALM KERNEL OLEIN

Lipase (triacylglycerol ester hydrolase, EC 3.1.1.3) from Rhizopus arr hizus was immobilized in this work by adsorption on microporous polypr opylene and employed for the lipolysis of palm kernel olein. The optim um operating temperature for the lipolysis reaction was determined. Th e reaction follows Michaelis-Menten kinetics with product competitive inhibition for substrate concentrations in the range of 0.175-0.877M. The apparent K-M and V-max were 0.42M and 691 U/mg protein, respective ly. A dissociation constant of the enzyme-product complex, K-I = 29.73 mM, for the product inhibition was also determined. Additionally, the time-courses of the reaction for various substrate concentrations wer e obtained and correlated sufficiently with those predicted from the t heoretical rate equation for a period of up to 2 h. Experimental resul ts indicated that discrepancies between the observed results and the p redicted ones increase with reaction time.