Kinetic Studies on Lipase-catalyzed Transesterification of Phosphatidylcholine with ?-linolenic Acid Ethyl Ester

Abstract

The kinetics of the transesterification of phosphatidylcholine (PC) with α-linolenic acid ethyl ester (ALAEE) catalyzed by immobilized lipase in hexane was studied. The reaction proceeded via a Ping-Ping Bi-Bi mechanism without inhibition by both the substrates at various concentrations tested. A reaction kinetic model was proposed with the experimental data. The kinetic constants of the model were determined at 45 o C, which were 1.2×10 -2 μmol.min -1 .mg -1 , 64.1 mM and 282.8 mM for Vmax, KmALA and KmPC, respectively.