Journal of Lipid Research, Vol. 10, 271-276, May 1969
Copyright © 1969 by Lipid Research, Inc.

Relative rates of hydrolysis by rat pancreatic lipase of esters of C₂-C₁₈ fatty acids with C₁-C₁₈ primary n-alcohols

F. H. Mattson and R. A. Volpenhein

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

The rate at which rat pancreatic lipase (glycerol-ester hydrolase, EC 3.1.1.3) hydrolyzes the esters of primary n-alcohols containing from 1 to 18 carbon atoms with fatty acids containing from 2 to 18 carbon atoms was determined. The speed of hydrolysis was influenced, apparently independently, by both the acyl and the alkyl chains. With respect to the fatty acid moiety, the esters of dodecanoic acid were usually split at the most rapid rate. Esters of butyric acid were the next most susceptible. In the case of the alcohol moiety, esters of heptyl alcohol were hydrolyzed most rapidly.

On the basis of the pattern of the relative rates of hydrolysis, it is proposed that the influence of the alcohol component is a result of its orienting the ester molecule at the oil/water interface. The fatty acid effect is attributed to enzyme-substrate specificity.

Supplementary key words substrate specificity • orientation at oil/water interface

Submitted on October 28, 1968
Accepted on January 15, 1969

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