Kinetic study of esterification by immobilized lipase in n-hexane.
The kinetic of the esterification of oleic acid by ethanol catalyzed by immobilized lipase of Mucor miehei in n-hexane as a solvent has been completely studied. The kinetics of the reaction are suggested to agree with a Ping-Pong Bi Bi mechanism in which only inhibition by excess of ethanol has been identified. Values of all apparent kinetic parameters were computed. No evidence of any significant external diffusional limitation which could account for these values has been detected. Optimization of water content through distribution ratio of water between solvent and support was examined.
Chulalaksananukul
W
W
Département de Génie Biochimique et Alimentaire, UA-CNRS 544, Institut National des Sciences Appliquées, Toulouse, France.
Condoret
J S
JS
Delorme
P
P
Willemot
R M
RM
D004800:Enzymes, Immobilized / Q000378:metabolism*; D004952:Esters; D000431:Ethanol / Q000494:pharmacology; D006586:Hexanes; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D009089:Mucor / Q000201:enzymology; D019301:Oleic Acid; D009829:Oleic Acids / Q000378:metabolism; D013816:Thermodynamics
D004800:Enzymes, Immobilized; D004952:Esters; D006586:Hexanes; D009829:Oleic Acids; C026385:n-hexane; D019301:Oleic Acid; D000431:Ethanol; D008049:Lipase