Lipase catalyzed transesterification of ethyl butyrate synthesis in n -hexane— a kinetic study

Abstract

Kinetics of lipase catalyzed transesterification of ethyl caprate and butyric acid was investigated. The objective of this work was to propose a reaction mechanism and develop a rate equation for the synthesis of ethyl butyrate by transesterification using surfactant coated lipase from Candida rugosa. The reaction rate could be described in terms of Michaelis–Menten equation with a Ping-Pong Bi–Bi mechanism and competitive inhibition by both the substrates. The values of kinetic parameters computed were V_max = 2.861 μmol/min/mg; K_m(acid) = 0.0746 M; K_m(ester) = 0.125 M; K_i acid = 0.450 M. This study indicated a competitive enzyme inhibition by butyric acid during lipase catalyzed transesterification reaction. Experimental observations had clearly indicated that the substrates as well as product act as dead-end inhibitors.

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