Lipase catalyzed transesterification of ethyl butyrate synthesis in n-hexane— a kinetic study

Kinetics of lipase catalyzed transesterification of ethyl caprate and butyric acid was investigated. The objective of this work was to propose a reaction mechanism and develop a rate equation for the synthesis of ethyl butyrate by transesterification using surfactant coated lipase from Candida rugos...

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Bibliographic Details
Published in:Journal of food science and technology 2017-08, Vol.54 (9), p.2871-2877
Main Authors: Devi, N. Annapurna, Radhika, G. B., Bhargavi, R. J.
Format: Article
Language:English
Subjects:
Acids
Butyric acid
Chemical synthesis
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Enzymes
Ethyl butyrate
Food Science
Kinetics
Lipase
n-Hexane
Nutrition
Original
Original Article
Reaction kinetics
Reaction mechanisms
Studies
Substrate inhibition
Substrates
Transesterification
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Summary:Kinetics of lipase catalyzed transesterification of ethyl caprate and butyric acid was investigated. The objective of this work was to propose a reaction mechanism and develop a rate equation for the synthesis of ethyl butyrate by transesterification using surfactant coated lipase from Candida rugosa . The reaction rate could be described in terms of Michaelis–Menten equation with a Ping-Pong Bi–Bi mechanism and competitive inhibition by both the substrates. The values of kinetic parameters computed were V max  = 2.861 μmol/min/mg; K m(acid)  = 0.0746 M; K m(ester)  = 0.125 M; K i acid = 0.450 M. This study indicated a competitive enzyme inhibition by butyric acid during lipase catalyzed transesterification reaction. Experimental observations had clearly indicated that the substrates as well as product act as dead-end inhibitors.
ISSN:0022-1155
0975-8402
DOI:10.1007/s13197-017-2725-2