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Altinelataman, Can; Koroleva, Olga; Fedorova, Tatyana; Torkova, Anna; Lisitskaya, Ksenia; Tsentalovich, Mikhail; Kononikhin, Aleksey; Popov, Igor; Vasina, Dania; Kovalyov, Leonid; Celik, Ufuk
{ "@context": "https://schema.org/", "@id": 67903, "@type": "ScholarlyArticle", "creator": [ { "@type": "Person", "affiliation": "Ege Univ, Fac Fisheries, TR-35100 Izmir, Turkey", "name": "Altinelataman, Can" }, { "@type": "Person", "affiliation": "Russian Acad Sci, Res Ctr Biotechnol, 33,Bld 2,Leninsky Ave, Moscow 119071, Russia", "name": "Koroleva, Olga" }, { "@type": "Person", "affiliation": "Russian Acad Sci, Res Ctr Biotechnol, 33,Bld 2,Leninsky Ave, Moscow 119071, Russia", "name": "Fedorova, Tatyana" }, { "@type": "Person", "affiliation": "Russian Acad Sci, Res Ctr Biotechnol, 33,Bld 2,Leninsky Ave, Moscow 119071, Russia", "name": "Torkova, Anna" }, { "@type": "Person", "affiliation": "Russian Acad Sci, Res Ctr Biotechnol, 33,Bld 2,Leninsky Ave, Moscow 119071, Russia", "name": "Lisitskaya, Ksenia" }, { "@type": "Person", "affiliation": "Russian Acad Sci, Res Ctr Biotechnol, 33,Bld 2,Leninsky Ave, Moscow 119071, Russia", "name": "Tsentalovich, Mikhail" }, { "@type": "Person", "name": "Kononikhin, Aleksey" }, { "@type": "Person", "name": "Popov, Igor" }, { "@type": "Person", "affiliation": "Russian Acad Sci, Res Ctr Biotechnol, 33,Bld 2,Leninsky Ave, Moscow 119071, Russia", "name": "Vasina, Dania" }, { "@type": "Person", "affiliation": "Russian Acad Sci, Res Ctr Biotechnol, 33,Bld 2,Leninsky Ave, Moscow 119071, Russia", "name": "Kovalyov, Leonid" }, { "@type": "Person", "affiliation": "Ege Univ, Fac Fisheries, TR-35100 Izmir, Turkey", "name": "Celik, Ufuk" } ], "datePublished": "2019-01-01", "description": "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.", "headline": "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", "identifier": 67903, "image": "https://aperta.ulakbim.gov.tr/static/img/logo/aperta_logo_with_icon.svg", "license": "http://www.opendefinition.org/licenses/cc-by", "name": "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", "url": "https://aperta.ulakbim.gov.tr/record/67903" }
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