J. Lipid Res.
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Journal of Lipid Research, Vol. 9, 79-84, January 1968
Copyright © 1968 by Lipid Research, Inc.

Hydrolysis of primary and secondary esters of glycerol by pancreatic juice

F. H. Mattson and R. A. Volpenhein

The Procter & Gamble Company, Miami Valley Laboratories, Cincinnati, Ohio 45239

The relative rates of hydrolysis of the secondary ester in glycerol 1,3-benzylidene 2-oleate and in glycerol 1,3-dihexadecyl ether 2-oleate, and of the primary and secondary esters in triolein were determined. Both unaltered and selectively inactivated rat pancreatic juice were used as sources of enzyme. It was found that rat pancreatic juice contains an enzyme that can hydrolyze fatty acids esterified at the 2-position of a glyceride. This enzyme is not pancreatic lipase. It may be sterol ester hydrolase. Partial glycerides, as well as complete glycerides, can serve as substrates. Pancreatic lipase, if it can hydrolyze the 2-positioned fatty acids of a triglyceride, does so at a very slow rate.

Supplementary key words enzyme specificity • digestion • absorption • pancreatic lipase • cholesterol esterase • structure of triglycerides

Submitted on August 10, 1967
Accepted on September 20, 1967


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