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 effic...
| Main Authors: | , |
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| Format: | Article in Journal/Newspaper |
| Language: | unknown |
| Published: |
American Chemical Society
2008
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| Subjects: | |
| Online Access: | http://repository.ias.ac.in/111656/ http://pubs.acs.org/doi/abs/10.1021/ie800193f |
| Summary: | 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. |
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