Bovine pancreatic lipase. III. Lipolysis of oils and fats and fatty acid specificity.
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 commericial vegetable oils. With regard to the lipolytic behavior, in general, the bovine pancreatic lipase closely resembled milk lipase.
D000818:Animals; D002079:Butter; D002417:Cattle; D005223:Fats / Q000378:metabolism*; D005227:Fatty Acids; D005989:Glycerides / Q000378:metabolism; D006868:Hydrolysis; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D008892:Milk; D009821:Oils / Q000378:metabolism*; D010179:Pancreas / Q000201:enzymology*; D013329:Structure-Activity Relationship
D005223:Fats; D005227:Fatty Acids; D005989:Glycerides; D009821:Oils; D002079:Butter; D008049:Lipase