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Lipolysis by a B-Esterase Preparation from Milk¹

Department of Animal Industries, Storrs Agricultural Experiment Station, Storrs, Connecticut

T. L. Forster

Department of Dairy Science, State University of Washington, Pullman, Washington

ABSTRACT

Milk contains enzymes capable of preferentially hydrolyzing the primary ester positions of the synthetic triglycerides, 2-oleyl dipalmitin and 2-palmitoyl diolein (3). Forster et al. (2) have demonstrated that milk also contains an enzyme, B-esterase, which hydrolyzes tributyrin and has been designated as an aliphatic esterase or lipase. The question arose, does B-esterase hydrolyze long-chain triglycerides in the same sequence as milk lipase? The preparation of a B-esterase concentrate from milk (8), by one of the authors (T.L.F.), permitted this question to be answered.

B-esterase concentrate was added at a level of between 1 and 3% to an emulsion of synthetically prepared 2-oleyl dipalmitin (3) in pasteurized skimmilk and the resulting mixture incubated for 30 min. in a water bath at 38° C. with shaking. After extraction and separation of the free fatty acids (3), these were identified as methyl esters by gas-liquid chromatography. (Aerograph Model A-90C.) The concentrations of palmitic and oleic acids were determined from the areas under the peaks on the charts by a disc integrator built into the recorder.

¹ This investigation was supported in part by research grant (A-2605) from the National Institute of Arthritis and Metabolic Diseases, Public Health Services.