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In vitro Antioxidant Effects of Porphyra haitanensis Peptides on H2O2-Induced Damage in HepG2 Cells

文献类型: 外文期刊

作者: Chen Shengjun 1 ; Yu Jiao 1 ; Hu Xiao 1 ; Yang Xianqing 1 ; Li Laihao 1 ; Qi Bo 1 ; Deng Jianchao 1 ;

作者机构: 1.Chinese Acad Fishery Sci, Key Lab Aquat Prod Proc, Minist Agr & Rural Affairs, Natl Res & Dev Ctr Aquat Prod Proc,South China Se, Guangzhou 510300, Peoples R China

2.Jiangsu Ocean Univ, Coinnovat Ctr Jiangsu Marine Bioind Technol, Lianyungang 222005, Peoples R China

3.Shanghai Ocean Univ, Coll Food Sci & Technol, Shanghai 201306, Peoples R China

关键词: Porphyra haitanensis hydrolysates (PHHs); antioxidant peptides; radical-scavenging activity; cell antioxidant capacity; electrospray ionization-mass spectrometry

期刊名称:JOURNAL OF OCEAN UNIVERSITY OF CHINA ( 影响因子:0.913; 五年影响因子:1.012 )

ISSN: 1672-5182

年卷期: 2021 年 20 卷 2 期

页码:

收录情况: SCI

摘要: In this study, protein from Porphyra haitanensis was used as raw material to prepare an antioxidant peptide, and its antioxidant activity was evaluated in vitro. A model of H2O2-induced oxidative damage in HepG2 cells was established, and the effects of Porphyra haitanensis hydrolysates (PHHs) on superoxide dismutase (SOD) activity and malondialdehyde (MDA) content were detected. Finally, the structure of PHHs was identified by ESI-MS/MS. The results showed that the 1,1-diphenyl-2-pyridylhydrazine (DPPH)-free radical-scavenging ability of PHHs was the strongest (59.28% at 1.0 mg mL(-1)) when hydrolyzed with an acidic protease for 4 h. PHHs with different concentrations had protective effects on H2O2-induced damage to HepG2 cells, and the protective effect was enhanced with increasing concentrations. When the level was 400 mu g mL(-1), the cell survival rate was as high as 88.62%. Moreover, PHHs can significantly reduce oxidative damage to HepG2 cells by H2O2, improve SOD activity, and reduce MDA content. The tetrapeptide Asp-Lys-Ser-Thr, with a molecular weight of 448 Da, was identified as an important fraction of PHHs by high-resolution mass spectrometry.

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