Human milk lipases and their possible role in fat digestion.

Human milk contains two lipases. One is a lipoprotein lipase with properties similar to the lipoprotein lipases that participate in the metabolism of blood plasma lipoproteins in several tissues. This enzyme is present in high activity in the lactating mammary gland where it facilitates the uptake of triglyceride fatty acids from the blood lipoproteins for production of milk lipids in the gland. The high activity of this enzyme in milk probably represent leakage of enzyme from the gland. This lipase is not stable at pH below 5 or in intestinal contents and it is unlikely that it participates in intestinal fat digestion. Its activity varies widely between individual milk samples, and there is a high correlation between its activity and the development of hydrolytic rancidity in the milk on storage. The other lipase is present in the milk in an inactive form which is activated by bile salts. This lipase is present in milk from primates but not in milk from lower animals. Human milk contains enough of this lipase to hydrolyze the milk lipids almost completely in less than half an hour at the pH and the bile acid and salt concentrations found in the small intestine of the human infant. It is probable that it increases the efficiency of milk fat absorption. The enzyme has a rather wide substrate specificity and may also act on other lipid substrates than triglycerides. In contrast to pancreatic lipase it hydrolyses all three ester bonds in a triglyceride. This may affect the physical chemistry of the lipids in the intestinal contents as well as their absorption and further metabolism in the musoca.