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Enzymatic synthesis of ethyl hexanoate by transesterification
Author(s) -
Chowdary G. V.,
Prapulla S. G.
Publication year - 2003
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1046/j.1365-2621.2003.00653.x
Subject(s) - rhizomucor miehei , chemistry , lipase , ethyl hexanoate , hexanoic acid , transesterification , substrate (aquarium) , organic chemistry , enzyme , triacylglycerol lipase , chromatography , ethyl acetate , catalysis , oceanography , geology
Summary Enzymatic synthesis of ethyl hexanoate by means of an acyl transfer reaction has been studied by using an immobilized Rhizomucor miehei lipase (RML). The effect of reaction parameters on ester synthesis has been investigated. Rhizomucor miehei lipase showed more specificity than other lipases when ethyl hexanoate was synthesized in n ‐hexane. Maximum ester synthesis was obtained by using a 0.5 m substrate concentration (equimolar ratio). Temperatures in the range of 45–55 °C were found to be optimum and at higher temperatures (>60 °C) deactivation of enzyme was observed. Higher molar concentrations of hexanoic acid inhibited RML, but no inhibitory effect of ethyl caprate, even at higher molar concentrations, was observed. Apparent kinetic parameters have been determined. The values are as follows: K M (ester), 0.0135 m ; K M (acid), 0.08466; K i (ester), 3.07 m ; K i (acid), 0.550 m ; V max , 1.861 µmol min −1 mg −1 enzyme.