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

• Main Authors: Yadav, Ganapati D., Borkar, Indrakant V.
• Format: Article in Journal/Newspaper
• Language: unknown
• Published: American Chemical Society 2008
• Subjects: T Technology (General); Antarc*; Antarctica
• Online Access: http://repository.ias.ac.in/111656/; http://pubs.acs.org/doi/abs/10.1021/ie800193f

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 tetra-butyl 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.