The presence of specific peptides with antioxidant properties released during carp protein ex vivo and in vitro hydrolysis by human/porcine digestive enzymes, respectively, was examined. Based on the results of the in silico data analysis, antioxidant peptides were selected for subsequent identification in the digests/hydrolysates. Carp proteins were more resistant to hydrolysis by porcine enzymes than by human digestive juices. The sarcoplasmic proteins were hydrolyzed faster than the myofibrillar ones by both human/porcine enzymes. The in vitro myofibrillar protein hydrolysate showed the highest ABTS(+) scavenging activity (∼232.3 TEAC, μM Trolox/g), whereas the ex vivo hydrolysate of sarcoplasmic proteins showed the highest DPPH scavenging activity (∼88μM/g) and reducing power. Five antioxidant peptides were identified in carp protein ex vivo and in vitro hydrolysates: FIKK, HL, IY, PW, VY. The peptide HL from myofibrillar proteins was identified only in the ex vivo hydrolysate, whereas the peptide PW from sarcoplasmic proteins was identified only in the in vitro hydrolysate.
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