Synergism between microwave irradiation and enzyme catalysis in transesterification of ethyl-3-phenylpropanoate with n-butanol

Lipase catalyzed transesterification was investigated to study the synergistic effect of microwave irradiation and enzyme catalysis. Transesterification of ethyl-3-phenylpropanoate with n-butanol was chosen as the model reaction using immobilized enzymes such as Novozyme 435, Lipozyme RMIM and Lipozyme TL IM with microwave irradiation. Novozyme 435 was the best catalyst. The effect of various parameters affecting the conversion and initial rates of transesterification were studied to establish kinetics and mechanism. There is synergism between enzyme catalysis and microwave irradiation. The analysis of initial rate data and progress curve data showed that the reaction obeys the Ping-Pong bi–bi mechanism with inhibition by n-butanol. The theoretical predictions and experimental data match very well. These studies were also extended to other alcohols such as 2-phenyl-1-propanol, n-octanol, benzyl alcohol, iso-amyl alcohol, 2-hexanol and 2-pentanol under otherwise similar conditions.

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► Lipase catalyzed transesterification of ethyl-3-phenylpropanoate in organic media.
► Immobilized Candida antarctica lipase B was found to be the best catalyst.
► There is synergism between enzyme catalysis and microwave irradiation.
► The Ping-Pong bi–bi mechanism with alcohol inhibition supports the reaction mechanism.
► Theoretical predications and experimental data match very well.