Stereospecificity of lipases. Enzymatic hydrolysis of enantiomeric alkyldiacyl- and dialkylacylglycerols by lipoprotein lipase.
Lipoprotein lipase from dialyzed and lyophilized bovine skim milk hydrolyses specifically the ester in position 1 of triacylglycerols and of enantiomeric alkyldiacylglycerols. No such specificity could be observed when enantiomeric dialkylacylglycerols were used as substrates since hydrolysis in positions 1 and 3 occurred at the same rate. Dialkylacylglycerols are, therefore, unsuitable as model substrates for the assay of the stereospecificity of lipases.
D000818:Animals; D002417:Cattle; D007700:Kinetics; D008071:Lipoprotein Lipase / Q000378:metabolism*; D008892:Milk / Q000201:enzymology; D013237:Stereoisomerism; D013329:Structure-Activity Relationship; D014280:Triglycerides
D014280:Triglycerides; D008071:Lipoprotein Lipase