1 Ocak 2019 Dergi makalesi Açık Erişim

Altinelataman, Can; Koroleva, Olga; Fedorova, Tatyana; Torkova, Anna; Lisitskaya, Ksenia; Tsentalovich, Mikhail; Kononikhin, Aleksey; Popov, Igor; Vasina, Dania; Kovalyov, Leonid; Celik, Ufuk

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    "creators": [
      {
        "affiliation": "Ege Univ, Fac Fisheries, TR-35100 Izmir, Turkey", 
        "name": "Altinelataman, Can"
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      {
        "affiliation": "Russian Acad Sci, Res Ctr Biotechnol, 33,Bld 2,Leninsky Ave, Moscow 119071, Russia", 
        "name": "Koroleva, Olga"
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      {
        "affiliation": "Russian Acad Sci, Res Ctr Biotechnol, 33,Bld 2,Leninsky Ave, Moscow 119071, Russia", 
        "name": "Fedorova, Tatyana"
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      {
        "affiliation": "Russian Acad Sci, Res Ctr Biotechnol, 33,Bld 2,Leninsky Ave, Moscow 119071, Russia", 
        "name": "Torkova, Anna"
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      {
        "affiliation": "Russian Acad Sci, Res Ctr Biotechnol, 33,Bld 2,Leninsky Ave, Moscow 119071, Russia", 
        "name": "Lisitskaya, Ksenia"
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      {
        "affiliation": "Russian Acad Sci, Res Ctr Biotechnol, 33,Bld 2,Leninsky Ave, Moscow 119071, Russia", 
        "name": "Tsentalovich, Mikhail"
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      {
        "name": "Kononikhin, Aleksey"
      }, 
      {
        "name": "Popov, Igor"
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      {
        "affiliation": "Russian Acad Sci, Res Ctr Biotechnol, 33,Bld 2,Leninsky Ave, Moscow 119071, Russia", 
        "name": "Vasina, Dania"
      }, 
      {
        "affiliation": "Russian Acad Sci, Res Ctr Biotechnol, 33,Bld 2,Leninsky Ave, Moscow 119071, Russia", 
        "name": "Kovalyov, Leonid"
      }, 
      {
        "affiliation": "Ege Univ, Fac Fisheries, TR-35100 Izmir, Turkey", 
        "name": "Celik, Ufuk"
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    ], 
    "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.", 
    "doi": "10.1016/j.foodchem.2018.08.004", 
    "has_grant": false, 
    "journal": {
      "pages": "724-732", 
      "title": "FOOD CHEMISTRY", 
      "volume": "271"
    }, 
    "license": {
      "id": "cc-by"
    }, 
    "publication_date": "2019-01-01", 
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    "resource_type": {
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      "title": "Dergi makalesi", 
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    "title": "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"
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