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Lipolysis of trivernolin by pancreatic lipase
Author(s) -
Sampugna J.,
Jensen R. G.,
Parry R. M.,
Krewson C. F.
Publication year - 1964
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/bf02673490
Subject(s) - lipase , lipolysis , monoglyceride , pancreatic lipase , chemistry , monoacylglycerol lipase , triglyceride , fatty acid , biochemistry , incubation , enzyme , adipose tissue , cholesterol , endocannabinoid system , receptor
Vernolic acid ( cis ‐12,13‐epoxy‐ cis ‐9‐oetadece‐noic acid) occurs as the triglyceride in the seed of Vernonia anthelmintica. Incubation of the seed produces a 1,3‐divernolin. To determine whether the structure of trivernolin is responsible for the apparent secondary ester position specificity of the natural enzyme, trivernolin and tri‐olein, were incubated with pancreatic lipase and the free fatty acids and monoglycerides were determined after 5 and 15 min digestion periods. The preponderance of 2‐monoglyceride produced by the action of pancreatic lipase was interpreted to indicate that the structure of trivernolin was not solely responsible for the secondary position specificity of the V. anthelmintica lipase toward trivernolin.