KINETICS OF LIPASE-CATALYZED INTERESTERIFICATION OF TRIGLYCERIDES IN CYCLOHEXANE

The kinetics of interesterification reactions catalysed by Candida cylindracea lipase in cyclohexane have been investigated. The enzymatic rate constants K(m) and V(max) have been measured for the hydrolysis of trilaurin and the esterification of dilaurin and lauric acid, in the absence of mass transfer limitations. The enzymatic turnover number for esterification is three times higher than that for hydrolysis, suggesting that hydrolysis may be the rate-controlling step in interesterification. Equations are presented for K(m) and V(max) in terms of elementary-step rate constants.