Studies on the substrate specificity of purified human milk lipoprotein lipase.
The fatty acid specificity of purified human milk lipoprotein lipase was studied using the C18 to C54 (total acyl carbon number) saturated and the C54 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.
D002849:Chromatography, Gas; D004075:Diglycerides / Q000378:metabolism; D005227:Fatty Acids / Q000378:metabolism*; D005231:Fatty Acids, Unsaturated / Q000378:metabolism; D005260:Female; D006801:Humans; D007700:Kinetics; D008071:Lipoprotein Lipase / Q000378:metabolism*; D008895:Milk, Human / Q000201:enzymology*; D013237:Stereoisomerism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D014280:Triglycerides / Q000378:metabolism
D004075:Diglycerides; D005227:Fatty Acids; D005231:Fatty Acids, Unsaturated; D014280:Triglycerides; D008071:Lipoprotein Lipase