A peptidomic analysis of human milk digestion in the infant stomach reveals protein-specific degradation patterns

David C. Dallas, Andrés Guerrero, Nora Khaldi, Robyn Borghese, Aashish Bhandari, Mark Underwood, Carlito B Lebrilla, J. Bruce German, Daniela Barile

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

In vitro digestion of isolated milk proteins results in milk peptides with a variety of actions. However, it remains unclear to what degree protein degradation occurs in vivo in the infant stomach and whether peptides previously annotated for bioactivity are released. This study combined nanospray LC separation with time-of-flight mass spectrometry, comprehensive structural libraries, and informatics to analyze milk from 3 human mothers and the gastric aspirates from their 4- to 12-d-old postpartum infants. Milk from the mothers contained almost 200 distinct peptides, demonstrating enzymatic degradation of milk proteins beginning either during lactation or between milk collection and feeding. In the gastric samples, 649 milk peptides were identified, demonstrating that digestion continues in the infant stomach. Most peptides in both the intact milk and gastric samples were derived from ß-casein. The numbers of peptides from ß-casein, lactoferrin, α-lactalbumin, lactadherin, κ-casein, serum albumin, bile salt-associated lipase, and xanthine dehydrogenase/oxidase were significantly higher in the gastric samples than in the milk samples (P < 0.05). A total of 603 peptides differed significantly in abundance between milk and gastric samples (P < 0.05). Most of the identified peptides have previously identified biologic activity. Gastric proteolysis occurs in the term infant in the first 2 wk of life, releasing biologically active milk peptides with immunomodulatory and antibacterial properties of clinical relevance to the proximal intestinal tract. Data are available via ProteomeXchange (identifier PXD000688).

Original languageEnglish (US)
Pages (from-to)815-820
Number of pages6
JournalJournal of Nutrition
Volume144
Issue number6
DOIs
StatePublished - 2014

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Human Milk
Proteolysis
Digestion
Stomach
Milk
Peptides
Caseins
Milk Proteins
Mothers
Xanthine Dehydrogenase
Lactalbumin
Informatics
Lactoferrin
Xanthine Oxidase
Bile Acids and Salts
Lipase
Lactation
Serum Albumin
Postpartum Period
Libraries

ASJC Scopus subject areas

  • Medicine (miscellaneous)
  • Nutrition and Dietetics

Cite this

A peptidomic analysis of human milk digestion in the infant stomach reveals protein-specific degradation patterns. / Dallas, David C.; Guerrero, Andrés; Khaldi, Nora; Borghese, Robyn; Bhandari, Aashish; Underwood, Mark; Lebrilla, Carlito B; Bruce German, J.; Barile, Daniela.

In: Journal of Nutrition, Vol. 144, No. 6, 2014, p. 815-820.

Research output: Contribution to journalArticle

Dallas, DC, Guerrero, A, Khaldi, N, Borghese, R, Bhandari, A, Underwood, M, Lebrilla, CB, Bruce German, J & Barile, D 2014, 'A peptidomic analysis of human milk digestion in the infant stomach reveals protein-specific degradation patterns', Journal of Nutrition, vol. 144, no. 6, pp. 815-820. https://doi.org/10.3945/jn.113.185793
Dallas, David C. ; Guerrero, Andrés ; Khaldi, Nora ; Borghese, Robyn ; Bhandari, Aashish ; Underwood, Mark ; Lebrilla, Carlito B ; Bruce German, J. ; Barile, Daniela. / A peptidomic analysis of human milk digestion in the infant stomach reveals protein-specific degradation patterns. In: Journal of Nutrition. 2014 ; Vol. 144, No. 6. pp. 815-820.
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