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Specificity of Milk Lipase for a Butyryl Triglyceride¹

Department of Animal Industries, University of Connecticut, Storrs

R. C. Chandan and K. M. Shahani

Department of Dairy Science, University of Nebraska, Lincoln

ABSTRACT

Milk lipase liberates relatively large quantities of butyric acid (4:0) from milk fat; 8.6% (methyl ester) in the FFA, as compared to 4.7% in the intact fat (3). In the past this has been attributed to specificity for short-chain acids. Yet, when a triglyceride (TG) such as glyceryl 1-palmitate 2,3-dibutyrate was used as a substrate for milk lipase, 4:0 and 16:0 were released in equimolar quantities (5). These results seem contradictory; a preferential release of 4:0, yet an absence of fatty acid specificity. We postulated that although milk lipase did not exhibit fatty acid or intramolecular specificity (defined as a major difference in rate of release of fatty acids occupying the 1- and 3- positions of glycerides), it did possess intermolecular specificity for TG's containing 4:0 as compared to long-chain TG's. Therefore, PBB and triolein (000) were mixed, digested, and the products analyzed to elucidate specificity. We have recently reported similar work with pancreatic lipase, which did not exhibit intramolecular specificity but did digest PBB more rapidly when this TG was mixed with glyceryl 1-myristate 2,3-dioleate (4).

¹ Scientific contribution No. 92, Agricultural Experiment Station, University of Connecticut, Storrs. Supported in part by Public Health Service Research grant AM-02605-06 from the Institute of Arthritis and Metabolic Diseases.