Identification of bioactive peptides after digestion of human milk and infant formula with pepsin and pancreatin |
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Affiliation: | 1. INRA, UMR 1253, Science et Technologie du Lait et de l''Oeuf, 65 Rue de St Brieuc, 35042 Rennes, France;2. Agrocampus Ouest, UMR 1253, Science et Technologie du Lait et de l''Oeuf, 65 Rue de St Brieuc, 35042 Rennes, France;3. Centre Hospitalier Universitaire de Rennes, Département de Pédiatrie, 16 Boulevard de Bulgarie, 35203 Rennes, France;4. CNRS, Aix Marseille Université, UMR 7282 Enzymologie Interfaciale & Physiologie de la Lipolyse, 31 Chemin Joseph Aiguier, 13402 Marseille, France |
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Abstract: | Seven human milks were subjected to an in vitro digestion with pepsin and pancreatin to identify the peptides released from human proteins. On the basis of their sequences, 11 of the 23 peptides were synthesised and their angiotensin converting enzyme (ACE)-inhibitory and antioxidant activities were measured. The β-casein peptides HLPLP and WSVPQPK showed potent ACE-inhibitory and antioxidant activity, with a protein concentration needed to inhibit 50% ACE activity (IC50) of 21 μm and a Trolox Equivalent Antioxidant Capacity (TEAC) of 1.297 μmol 6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid (Trolox) equivs μmol−1 of peptide, respectively. These activities were determined after digestion of eight infant formulas and compared with those found in digested human milk. One of the infant formulas exhibited a low IC50 value (60.11 μg protein mL−1 of reconstituted formula) and a high TEAC value (1.7056 μmol Trolox equivs mg−1 of protein) and was therefore selected to identify the peptides responsible of these activities. |
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