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Phylogeny of lipase specificity
Author(s) -
Berner David L.,
Hammond Earl G.
Publication year - 1970
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02532745
Subject(s) - tributyrin , lipase , clinical chemistry , biochemistry , triacylglycerol lipase , biology , hydrolysis , lipidology , chromatography , fatty acid , acetone , food science , chemistry , enzyme
Lipase preparations from 19 animal species, representing nine of the animal phyla, were studied. Acetone powders were prepared from the pancreas, hepatopancreas, gastrointestinal tract or whole animal, and the preparations were screened for lipolytic activity by tributyrin agar clearing. The pH optimum of each preparation was determined by using both tributyrin and corn oil emulsions. The positional specificity at the pH optimum of each lipase preparation was determined from the fatty acids released by a 2–5 min reaction with cocoa butter and lard. The vertebrate lipases behaved analogously to hog pancreatic lipase by showing a high specificity for the 1 and 3 positions of long chain triglycerides. Invertebrate preparations that did hydrolyze long chain triglycerides did so randomly, with no strong positional or fatty acid specificity.