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

WOS: 000444967800090PubMed ID: 30236737European 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.Scientific and Technological Research Council of Turkey, Turkey (TUBITAK)Turkiye Bilimsel ve Teknolojik Arastirma Kurumu (TUBITAK) [2219]; Russian Science Foundation, RussiaRussian Science Foundation (RSF) [14-24-00114]We wish to acknowledge The Scientific and Technological Research Council of Turkey, Turkey (TUBITAK) for support of Dr. Can Altinelataman by Grant # 2219 to join studies in Moscow. The part of research related to peptides identification by high resolution mass spectrometry measurements was supported by the Russian Science Foundation, Russia (Grant # 14-24-00114). This study was dedicated to memory of Prof. Dr. Olga Koroleva