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Journal of Dairy Science Vol. 59 No. 7 1203-1214
© 1976 by American Dairy Science Association ®
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Milk Lipoprotein Lipases: A Review1

Robert G. Jensen and Robert E. Pitas

Department of Nutritional Sciences, University of Connecticut, Storrs 06268

ABSTRACT

Lipoprotein lipase activity has been found in the milks from several species where it is assumed to result from leakage from the mammary gland into milk. The function of the enzyme in the gland is apparently to assist in the transfer of blood lipoprotein triacylglycerol fatty acids into milk triacylglycerols. Bovine skim milk is one of the richest sources of lipoprotein lipase and this enzyme has been purified extensively (7000 fold) by affinity chromatography. The lipase has a molecular weight of about 62000, is inhibited by protamine sulfate, 1.0 M sodium chloride, apolipoprotein C-I (apolipoprotein-serine), and apolipoprotein C-III (apolipoprotein-alanine). The enzyme is activated by apolipoprotein C-II (apolipoprotein-glutamic acid), serum, and by heparin to which it also binds. The lipase is highly specific for the primary esters of acylglycerols and exhibits a slight stereospecificity for the sn-1 ester in preference to the sn-3-ester. Bovine milk also has separate activity toward 1-monoacylglycerols. Human milk contains a serum stimulated lipoprotein lipase with many of the characteristics of the enzyme in bovine milk, as well as an enzyme stimulated by bile salts which resembles the sterol ester hydrolase of rat pancreatic juice. The assay, function, purification, characteristics, and substrate specificities of these enzymes are discussed.

FOOTNOTES

1 Scientific contribution 642, Agricultural Experiment Station, University of Connecticut, Storrs 06268.






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Copyright © 1976 by the American Dairy Science Association ®.