Kinetic modeling of immobilized lipase catalysis in synthesis of n-butyl levulinate

n-Butyl levulinate is used as an important intermediate having diverse applications. The present work focuses on the synthesis of n-butyl levulinate by esterification of levulinic acid with n-butanol by using immobilized lipases. Novozym 435 (Candida antarctica lipase) was found to be the most efficient catalyst, and tetrabutyl methyl ether was the best solvent. Effects of various parameters were studied to analyze the kinetics and mechanism of the lipase action. Ping-pong bi-bi mechanism with n-butanol substrate inhibition was found to describe the kinetics of the reaction. The kinetic parameters evaluated from initial rate data were used to simulate the experimental results. There was a very good agreement between theory and experiment.