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Some Evidence Supporting the Specificity of Milk Lipases for the Primary Hydroxyl Positions of Milk Glycerides¹

Storrs (Connecticut) Agricultural Experiment Station

ABSTRACT

Pancreatic lipase has been shown to hydrolyze triglycerides to 2-monoglycerides (MG's), which will eventually isomerize to 1-MG's (7, 8, 9). Thus, pancreatic lipase specifically hydrolyzes the primary hydroxyl positions of glycerides. Information on this subject is almost completely lacking for milk lipases. The problem can be attacked in several ways, one of which involves the determination of 1- and 2-MG's in lipolyzed milk fat. From the relative concentrations the sequence of lipolysis can be ascertained, under certain circumstances. However, the isomerization of 2-MG to the 1-isomer, which is catalyzed by acid, heat, alkali, and chromatographic separation on silica-gel columns, complicates the picture (1, 2, 6). An equilibrium mixture of about 90% 1-MG and 10% 2-isomer eventually will be obtained (6). In a previous paper (5) 2-MG's were found in lipolyzed milk, but the concentrations of the 1- and 2-isomers were such that no conclusions could be made as to specificity, probably because isomerization occurred during storage of the milk samples at 4° C. for 24 hr.

¹ This investigation was supported in part by a PHS research grant (A-2605 C1) from the National Institute of Arthritis and Metabolic Diseases, Public Health Service.