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The aim of this work was to investigate the presence of antioxidant and ACE-inhibitory activity in ovine αs2-casein and bovine κ-casein hydrolysates with antibacterial activity. Several pep- tides which had been previously identified in these hydrolysates were selected in order to fulfil cer- tain structural requirements and they were chemically synthesised to evaluate their antioxidant and ACE-inhibitory activity. Hydrolysates of ovine αs2-casein and bovine κ-casein with pepsin strongly inhibited ACE activity, with IC50 values of 41.8 and 9.97 μmol·L −1 , respectively. The κ-casein hy- drolysate also exhibited a significant oxygen radical absorbance capacity, seven times higher than that of Trolox. From the chemically synthesised peptides, two of them, LKKISQ and PYVRYL, both from ovine αs2-casein, exerted potent ACE-inhibitory activity in the range of the most po- tent food-derived antihypertensive peptides described to date (IC50 values of 2.6 and 2.4 μmol·L −1 , respectively). The latter sequence, corresponding to the C-terminal hexapeptide of the ovine αs2- casein molecule, also had antioxidant activity. The activity found is discussed in relation to the peptide sequences. αs2-casein / κ-casein / antibacterial activity / antioxidant activity / angiotensin-converting enzyme-inhibitory activity / bioactive peptide

Casein hydrolysates as a source of antimicrobial, antioxidant and antihypertensive peptides