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Studies on the substrate specificity of purified human milk lipoprotein lipase
Author(s) -
Wang C. S.,
Kuksis A.,
Manganaro F.
Publication year - 1982
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/bf02534942
Subject(s) - triolein , chemistry , lipase , lipolysis , hydrolysis , lipoprotein lipase , substrate (aquarium) , chromatography , triacylglycerol lipase , biochemistry , enzyme , organic chemistry , biology , adipose tissue , ecology
Abstract The fatty acid specificity of purified human milk lipoprotein lipase was studied using the C 18 to C 54 (total acyl carbon number) saturated and the C 54 mono‐, di‐ and triunsaturated monoacid triacylglycerols. Kinetic determinations indicated that the medium‐chain triacylglycerols were better substrates than long‐ or very short‐chain saturated triacylglycerols. The unsaturated triacylglycerols were hydrolyzed at rates comparable to that of tricaprylin with triolein having the highest rate of hydrolysis of the unsaturated species tested. The enzyme attacked the primary ester bond much more readily than the secondary ester bond. The purified human milk lipoprotein lipase showed a preferential stereospecific lipolysis of the sn ‐1‐position of the triacylglycerol molecule.