Esterification of fatty acids using nylon-immobilized lipase in n-hexane: kinetic parameters and chain-length effects

Zaidi, A; Gainer, JL; Carta, G; Mrani, A; Kadiri, T; Belarbi, Y; Mir, A

HERO ID

4944135

Reference Type

Journal Article

Year

2002

Language

English

PMID

11755985

HERO ID 4944135
In Press No
Year 2002
Title Esterification of fatty acids using nylon-immobilized lipase in n-hexane: kinetic parameters and chain-length effects
Authors Zaidi, A; Gainer, JL; Carta, G; Mrani, A; Kadiri, T; Belarbi, Y; Mir, A
Journal Journal of Biotechnology
Volume 93
Issue 3 (Feb 28
Page Numbers 209-216
Abstract 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 60 mmol h super(-1) g super(-1) immobilized enzyme when the substrates were present in equimolar proportions at an initial concentration of 0.6 mol l super(-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.
Doi 10.1016/s0168-1656(01)00401-1
Pmid 11755985
Wosid WOS:000173575200003
Is Certified Translation No
Dupe Override No
Comments Scopus URL: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037186284&doi=10.1016%2fS0168-1656%2801%2900401-1&partnerID=40&md5=631f8f3a78de547ed0d92fadd8171d7f
Is Public Yes
Language Text English
Keyword Candida rugosa; Triacylglycerol lipase; Fatty acids; Esterification; n-Hexane; Immobilized enzymes; 2002)