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Further characterization of the bile salt‐stimulated lipase in human milk
Author(s) -
Bläckberg Lars,
Hernell Olle
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80571-7
Subject(s) - lipase , chemistry , enzyme , lipoprotein lipase , biochemistry , salt (chemistry) , size exclusion chromatography , digestion (alchemy) , triacylglycerol lipase , breast milk , substrate (aquarium) , chromatography , biology , organic chemistry , ecology
Bile salt‐stimulated lipase is a milk enzyme unique to the higher primates. Its molecular and kinetic characteristics differ greatly from other lipolytic enzymes; e.g., pancreatic lipase and lipoprotein lipase. It has a much higher app. M r , 310 000 on gel filtration and 100 000 after denaturation. It requires primary bile salts for optimal activity and bile salts also protect the enzyme from proteolytic and heat inactivation. It may, due to its low substrate specificity, contribute to the utilization of a variety of milk lipids. Since it lacks positional specificity, digestion of milk triglycerides should be complete, which may explain why fat absorption is more efficient in breast‐fed than in formula‐fed infants.