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    Mother's milk contains proteases that release beneficial peptides from milk proteins. These milk proteases aid infant digestion, especially when the infant's own digestive capacity is low.

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    Area of Science:

    • Biochemistry
    • Immunology
    • Pediatrics

    Background:

    • Milk proteins possess inherent biological activities beyond nutrition.
    • Intact milk proteins contain encrypted functional sequences that yield bioactive peptides upon release.
    • These bioactive peptides exhibit antimicrobial and immunomodulatory properties, potentially aiding infant development.

    Purpose of the Study:

    • To investigate the origin and activity of proteases responsible for releasing functional peptides from milk proteins.
    • To determine the role of milk proteases in the digestion of milk proteins within the infant's gastrointestinal tract.
    • To elucidate the coordinated action of milk and infant proteases in releasing bioactive peptides.

    Main Methods:

    • Analysis of protease activity in human milk.
    • In vitro digestion studies using milk proteins and infant gastric conditions.
    • Identification of bioactive peptides released through proteolytic action.

    Main Results:

    • Functional peptide release begins within the mammary gland, mediated by milk proteases.
    • Milk proteases remain active in the infant's stomach, contributing significantly to milk protein digestion.
    • Milk proteases may supplement the neonate's limited digestive capacity.

    Conclusions:

    • A sophisticated system of milk and infant proteases facilitates the coordinated release of functional peptides from milk proteins.
    • Understanding this protein-protease-based peptide release system offers insights into early infant nutrition and immunity.
    • Further research is needed to fully understand the selective advantages of this system.