Identification of bioactive peptides after digestion of human milk and infant formula with pepsin and pancreatin

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.