- A kinetic study of immobilized lipase catalysing the synthesis of isoamyl acetate by transesterification in n-hexane.
A kinetic study of immobilized lipase catalysing the synthesis of isoamyl acetate by transesterification in n-hexane.
Enzyme and microbial technology (1992-09-01)
M Rizzi, P Stylos, A Riek, M Reuss
PMID1368893
RESUMEN
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.
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