A kinetic study of immobilized lipase catalysing the synthesis of isoamyl acetate by transesterification in n-hexane.

Isoamyl acetate was synthesized by lipase-catalyzed transesterification of ethyl acetate in n-hexane. The selectivity and rates of ester formation decreased when water content of the immobilized enzyme exceeded 3% (w/w). Experimental observations clearly indicate that the substrates as well as the product (ethanol) act as dead-end inhibitors. A ping-pong bi-bi mechanism with competitive inhibition by substrates and products is proposed that predicts the experimental observation satisfactorily.