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Bovine Pancreatic Lipase¹.III. Lipolysis of Oils and Fats and Fatty Acid Specificity

Department of Food Science and Technology, University of Nebraska, Lincoln 68503

ABSTRACT

Purified bovine pancreatic lipase hydrolyzed butteroil, vegetable oils, and synthetic glycerides. The enzyme hydrolyzed triglycerides more rapidly than di- and monoglycerides and tripropionin faster than any other synthetic glyceride. Triacetin was the least hydrolyzed glyceride. Gas-liquid chromatographic analysis of the free fatty acids liberated by the lipase from milk fat indicated that the enzyme selectively liberated butyric acid in higher proportion than the relative amount originally in the fat. The enzyme released saturated as well as unsaturated fatty acids from commercial vegetable oils. With regard to the lipolytic behavior, in general, the bovine pancreatic lipase closely resembled milk lipase.

¹ Published with the approval of the Director as Paper No. 3931, Journal Series, Agricultural Experiment Station, Lincoln, NE. Research work was conducted on Project 16-17. This study was supported in part by grants from American Dairy Association and Dairy Research, Inc. (DRINC).

² Purity Cheese Company, Mayville, WI 5 3050.

³ The Cary Memorial Hospital, 3 3 Lyndon Street, Caribou, ME 04736.