Journal of Lipid Research, Vol. 13, 777-782, November 1972
Copyright © 1972 by Lipid Research, Inc.

Digestion in vitro of erythritol esters by rat pancreatic juice enzymes

F. H. Mattson and R. A. Volpenhein

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

The mechanism of the digestion of erythritol esters was determined using rat pancreatic juice and purified pancreatic lipase (EC 3.1.1.3). Conditions of hydrolysis were used that would selectively activate or inactivate nonspecific lipase or lipase. It was shown that erythritol tetraoleate was hydrolyzed by nonspecific lipase but not by lipase. The initial digestion product was a triester, predominantly erythritol-1,2,3-trioleate. Thus, nonspecific lipase preferentially hydrolyzed the ester of a primary alcohol. In contrast to the results obtained with the tetraester, lipase could remove a fatty acid from the triester but the resulting erythritol-2,3-dioleate was not hydrolyzed by lipase. The selectivity of this hydrolysis and the inability to hydrolyze the diester are attributed to the known specificity of this enzyme to act only on esters of primary alcohols. Nonspecific lipase completely hydrolyzed erythritol tetraoleate to free erythritol in a stepwise manner. The relative rates of these reactions were

tetraester triester diester monoester erythritol

Because of the specificity of pancreatic lipase and the lack of specificity of nonspecific lipase it is likely that this latter enzyme is the primary agent for the hydrolysis of erythritol esters in the intact animal.

Supplementary key words erythritol tetraoleate • erythritol partial esters • thin-layer and column chromatography • pancreatic lipase • pancreatic nonspecific lipase • synthesis of erythritol-1,2,3-trioleate

Submitted on May 22, 1972
Accepted on August 3, 1972

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