Hydrolysis of triacylglycerol arachidonic and linoleic acid ester bonds by human pancreatic lipase and carboxyl ester lipase

Biochim Biophys Acta. 1989 Aug 22;1004(3):372-85. doi: 10.1016/0005-2760(89)90086-6.


The hydrolysis of polyenoic fatty acid ester bonds with pure human colipase-dependent lipase, with carboxyl ester lipase (CEL) and with these enzymes in combination was studied, using [3H]arachidonic- and [14C]linoleic acid-labelled rat chylomicrons as a model substrate. During the hydrolysis with colipase-dependent lipase, the amount of 3H appearing in 1,2-X-diacylglycerol (DG) markedly exceeded that of 14C. When CEL was added in addition this [3H]DG was efficiently hydrolyzed. CEL alone hydrolyzed the triacylglycerol (TG) at a low rate. The hydrolysis pattern with human duodenal content was similar to that seen with colipase-dependent lipase and CEL in combination. Increasing the concentration of taurodeoxycholate (TDC) and taurocholate (TC) or of TDC alone stimulated the hydrolysis of [3H]- and [14C]TG, but increased the accumulation of labelled DG that could act as substrate for CEL. It is suggested that very-long-chain polyenoic fatty acids of DG formed during the action of the colipase-dependent lipase on TG containing these fatty acids may be a physiological substrate for CEL.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arachidonic Acid
  • Arachidonic Acids / metabolism
  • Bile Acids and Salts / pharmacology
  • Carboxylesterase
  • Carboxylic Ester Hydrolases / physiology*
  • Chylomicrons / metabolism
  • Humans
  • Hydrolysis
  • In Vitro Techniques
  • Linoleic Acid
  • Linoleic Acids / metabolism
  • Lipase / physiology*
  • Pancreas / enzymology
  • Time Factors
  • Triglycerides / metabolism*


  • Arachidonic Acids
  • Bile Acids and Salts
  • Chylomicrons
  • Linoleic Acids
  • Triglycerides
  • Arachidonic Acid
  • Linoleic Acid
  • Carboxylic Ester Hydrolases
  • Carboxylesterase
  • Lipase