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BACKGROUND The 13S globulin is the main component of buckwheat seed storage proteins. In this study, tartary buckwheat 13S globulin was separated and its structural features were investigated using Edman sequencing and Matrix-Assisted Laser Desorption/Ionization Time of Flight Mass Spectrometry (MALDI-TOF-MS). Further, the protective effect of its enzymatic hydrolysates against oxidative stress induced by H2 O2 was evaluated to elucidate the antioxidant mechanism. RESULTS Results showed that the isolated tartary buckwheat 13S globulin contained one acidic and one basic subunit which were linked by a disulfide bond. Six tartary buckwheat active peptides were obtained from the enzymatic hydrolysates of tartary buckwheat 13S globulin acidic subunit with a molecule weight of 38 kDa, namely Pep-1, Pep-2, Pep-3, Pep-4, Pep-5, and Pep-6. Pre-treatment of cells with tartary buckwheat active peptides maintained the redox state balance of HepG2 cells and protected the activity of antioxidant enzymes in HepG2 cells. The tartary buckwheat active peptides improved oxidative stress in HepG2 cells via the PPAR-α/HO-1 pathway. CONCLUSION These results provide an insight into the antioxidant mechanism of tartary buckwheat 13S globulin and suggest that tartary buckwheat active peptides can be used as a functional ingredient in the food industry. This article is protected by copyright. All rights reserved.