An in vitro and in silico study on the antioxidant and cell culture-based study on the chemoprotective activities of fish muscle protein hydrolysates obtained from European seabass and gilthead seabream

European seabass (Dicentrarchus labrax, Linnaeus, 1758) (L) and gilthead seabream (Spares aurata, Linnaeus, 1758) (C) muscles were hydrolysated by Alcalase (L-alc, C-alc) and Chymotrypsin (L-ch, C-ch) then hydrolysates were examined and their peptide profiles obtained. A total of 765, 794, 132 and 232 peptides were identified in C-alc, L-alc, C-ch, and L-ch, respectively. Although, L-ch and C-ch, were expected to have more antioxidant capacity because of their peptide profiles, Alcalase hydrolysates observed in vitro, were slightly higher (TEAC assay for C-alc: 848.11 +/- 60.78 cool TE/g protein). Maximum inhibition of oxidative stress was determined for L-alc (12.8% +/- 4.5%) in MDCK1 cell lines. Highest proliferative capacity observed for C-alc (147.0% +/- 3.1%) at MTT assay in MDCK1 cell culture. L-ch showed the highest chemopreventive effect with a 40-60% decrease for human colon adenocarcinoma cell line HT-29. This research points out the importance of aquatic sources as raw materials for peptide researches.