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Lipolysis of Synthetic Triglycerides and Milk Fat by a Lipase Concentrate from Milk¹

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

K. M. Shahani and R. C. Chandan

Department of Dairy Husbandry, University of Nebraska, Lincoln

ABSTRACT

Investigations of unconcentrated milk lipases have revealed that these enzymes preferentially attack the primary ester positions of triglycerides (3–5). A more concentrated milk lipase, B-esterase (21 times on protein N), resembled unconcentrated milk lipase in lipolytic behavior (6) and, in addition, did not show specificity for short-chain acids when synthetic triglycerides containing both long- and short-chain acids were used as substrates (8). Although these studies have yielded information on the action of milk lipase, it is preferable to use highly purified preparations when studying enzyme specificity and reaction rates. Chandan and Shahani (1) have made available a more highly concentrated milk lipase (88 times on protein N) which showed essentially a single homogeneous protein moiety in ultracentrifuge studies and in moving boundary and gel electrophoresis. The availability of this highly purified milk lipase encouraged study of its lipolytic habits, using as substrates milk fat, olive oil, and synthetic triglycerides, so that comparisons of the three forms could be made.

¹ Supported in part by NIH research grant A-2605.