Lipase-catalyzed interesterification reaction between menhaden oil and the ethyl ester of CLA: Uniresponse kinetics

The kinetics of the interesterification reaction between menhaden oil and the ethyl ester of CLA (CLAEE) in the presence of an immobilized lipase from Rhizomucor miehei was investigated. A 2(3) factorial design with a central point was used to define the experimental region. The factors considered were the molar ratio of reactants, the enzyme loading, and the temperature. Optimal results were obtained when the reaction was carried out at 55degreesC with an enzyme loading of 0.65 g per 12 g mixture and a mole ratio of CLAEE to menhaden oil equal to 0.13. A uniresponse kinetic model of the Michael is-Menten type was developed to characterize the rate of consumption of CLAEE and the rate of release of FA ethyl esters from menhaden oil. The best fit of the data with a uniresponse model was obtained using a form based on reversible reactions and inhibition by the ethyl esters of the FA residues released by the reaction.