Abstract
Freudenberg was the first to show that human milk contains a lipase that is stimulated by bile salts1. Presence of this enzyme in gorilla milk2 and its absence in the milk of several other species (rat, guinea pig, rabbit, goat, cow, pig, dog, horse and rhesus monkey 2,3) were subsequently reported. Dependency on bile salts was not characteristic of lipase activity identified in the milk of many species as lipoprotein lipase4,5, an enzyme stimulated by a serum cofactor (apoprotein CII) and inhibited by bile salts5. However, while lipoprotein lipase has a key role in the mammary gland, where it regulates the uptake of long chain triglyceride-fatty acids from the circulation6, and thereby controls their concentration in milk, the enzyme has no known function in milk. The bile salt stimulated lipase, on the other hand, mav be an important compensatory digestive enzyme in the newborn infant7–9. Because of low pancreatic function at birth, the newborn depends on extrapancreatic lipases for the digestion of fatf8. Several studies have measured bile salt stimulated lipase activity throughout lactation in human milk and have investigated the characteristics of the enzyme purified from human milk8,10–12.
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© 1986 Plenum Press, New York
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Freed, L.M. et al. (1986). Bile Salt Stimulated Lipase: The Enzyme is Present in Non Primate Milk. In: Hamosh, M., Goldman, A.S. (eds) Human Lactation 2. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-7207-7_53
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DOI: https://doi.org/10.1007/978-1-4615-7207-7_53
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