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Bioactive peptides derived from human milk proteins: an update

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LIPPINCOTT WILLIAMS & WILKINS
DOI: 10.1097/MCO.0000000000000642

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bioactive peptides; gastrointestinal digestion; high-resolution mass spectrometry; human milk proteins

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Purpose of review Human milk contains a variety of bioactive proteins, and some of the bioactivities are exerted only after proteins are digested in the gastrointestinal tract. This review aims to overview recent studies on bioactive peptides in human milk and gastric digesta of breast-fed infants. Recent findings Milk protein-derived peptides are endogenously present in human milk, and some of them have been reported to be bioactive peptides, such as a homologue of caseinophosphopeptide, an antimicrobial peptide, and an immunomodulatory peptide. A larger number of peptides are identified in gastric aspirates from breast-fed infants, and bioactive peptides such as angiotensin I-converting enzyme-inhibitory peptides, an antioxidative peptide, opioid agonist peptides are only found in the digesta of human milk but not in human milkper se. Casein is the greatest source of released bioactive peptides. Technological advances have considerably increased our capability to identify and characterize peptides derived from human milk proteins. However, their physiological significance and the roles of these bioactive peptides in growth and development of breast-fed infants have not yet been sufficiently elucidated, and further in-vivo experiments and clinical trials are warranted.

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