Esterification of fatty acids using nylon-immobilized lipase in n-hexane: kinetic parameters and chain-length effects.
The esterification of long-chain fatty acids in n-hexane catalyzed by nylon-immobilized lipase from Candida rugosa has been investigated. Butyl oleate (22 carbon atoms), oleyl butyrate (22 carbon atoms) and oleyl oleate (36 carbon atoms) were produced at maximum reaction rates of approximately equal to 60 mmol h(-1) g(-1) immobilized enzyme when the substrates were present in equimolar proportions at an initial concentration of 0.6 mol l(-1). The observed kinetic behavior of all the esterification reactions is found to follow a ping-pong bi-bi mechanism with competitive inhibition by both substrates. The effect of the chain-length of the fatty acids and the alcohols could be correlated to some mechanistic models, in accordance with the calculated kinetic parameters.
Zaidi
A
A
Department of Chemical Engineering, Center for Bioprocess Development, University of Virginia, Charlottesville, VA 22903-2442, USA. zaidi@emi.ac.ma
Gainer
J L
JL
Carta
G
G
Mrani
A
A
Kadiri
T
T
Belarbi
Y
Y
Mir
A
A
D000269:Adhesives / Q000737:chemistry; D002175:Candida / Q000201:enzymology; D004800:Enzymes, Immobilized / Q000737:chemistry*; D004951:Esterification; D005227:Fatty Acids / Q000737:chemistry*; D006586:Hexanes / Q000737:chemistry*; D007700:Kinetics; D008049:Lipase / Q000737:chemistry*; D009757:Nylons / Q000737:chemistry*; D013816:Thermodynamics
D000269:Adhesives; D004800:Enzymes, Immobilized; D005227:Fatty Acids; D006586:Hexanes; D009757:Nylons; C026385:n-hexane; D008049:Lipase