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Comparative study of bioactive peptides released from in vitro digestion of human milk and infant formulas (623.1)
Author(s) -
Wada Yasuaki,
Lönnerdal Bo
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.623.1
Subject(s) - digestion (alchemy) , infant formula , chemistry , in vitro , peptide , food science , hydrolysis , pasteurization , biochemistry , chromatography
Human milk (HM), donor HM, and/or infant formulas (IFs) are the diets of most neonates. Bioactive peptides are known to be formed during gastrointestinal digestion of milk proteins, but the extent to which this occurs is not clear. HM, pasteurized HM (simulating donor HM), standard IF, and hypo‐allergenic IFs were subjected to in vitro digestion, followed by LC‐MS/MS analysis for identifying bioactive peptides. HM, where some peptides were present prior to digestion, released practically the same pattern of bioactive peptides with and without pasteurization, suggesting that provision of donor HM may be similar to breast‐feeding in terms of bioactive peptides, especially anti‐oxidative and ACE‐inhibitory peptides. Sequences of bioactive peptides were different between HM and standard IF, which may result in bioactivities with different intensity. Bioactive peptides formed from digestion of hypo‐allergenic IFs were less diverse than those from standard IF, indicating that industrial hydrolysis of cow’s milk protein for hypo‐allergenicity may impair the ‘encrypted’ bioactivities of the milk proteins. Further investigations in infants are needed to evaluate the bioactivities of the peptides.