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Journal of Dairy Science Vol. 83 No. 3 371-377
© 2000 by American Dairy Science Association ®
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Interesterification (Acidolysis) of Butterfat with Conjugated Linoleic Acid in a Batch Reactor

H. S. Garcia 1, K. J. Keough 2, J. A. Arcos 2, and C. G. Hill Jr. 2

1 Instituto Technológico de Veracruz, Apdo. Postal 1420, Veracruz, Ver. Meéxico
2 Department of Chemical Engineering, University of Wisconsin-Madison, 1415 Engineering Dr. Madison, WI 53706

Six commercial lipases, in free or immobilized form, were tested for their ability to catalyze acyl exchange between conjugated linoleic acid and anhydrous butterfat under solvent-free conditions. Immobilized Candida antarctica lipase exhibited the best activity. Experiments were conducted for this lipase in butterfat to conjugated linoleic acid ratios of 10:1 (vol/vol), temperatures from 30 to 70°C, enzyme concentrations of 50 to 200 mg/g of reaction mixture, and water contents of 0.15 to 2% (wt/wt). At the maximum enzyme concentration used, equilibrium was reached within the first 24 h of reaction. The optimum temperature was 50°C. The triacylglycerol profile of the product butterfat reflected changes in the relative proportions of fatty acid residues as the reaction proceeded, with increases in those triacylglycerols containing 46 to 54 carbon atoms and concomitant decreases in those triacylglycerols containing 34 to 42 carbon atoms.

Key Words: conjugated linoleic acid • butterfat • acidolysis • interesterification

Submitted on June 14, 1999
Accepted on September 21, 1999




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