LIPASE-CATALYZED ESTERIFICATION OF OLEIC-ACID AND METHANOL IN HEXANE - A KINETIC-STUDY

The kinetics of immobilized lipase-catalyzed esterification of oleic acid and methanol in hexane were investigated. The reaction follows Michaelis-Menton kinetics as observed from the relationship of initial rate of the reaction, both as a function of enzyme and of substrate concentration. Inhibition by excess of methanol has been identified. The kinetic constants have been measured for the reaction in the absence of any significant external diffusional limitations. The kinetics of the enzymatic reaction are suggested to agree with a Ping Pong Bi Bi mechanism.