Lipolysis of Laurate Glycerides by Pancreatic and Milk Lipase

Trilamin, 1,3-dilaurin, and 1-and 2-monolaurins were lipolyzed by pancreatic and purified milk lipases. Rates of digestion of the substrates decreased in the order listed above. Acyl migration was noted when 2-monolaurin was the substrate. The crude pancreatic lipase preparation may have contained other lipases as both 1-and 2-nmnolaurins were hydrolyzed. Significance of the findings with regard to the study of triglyeeride structure is discussed.