In this study, the antioxidant activity of mungbean protein hydrolysate (MPH) was systematically investigated. MPH was fractionated by ultrafiltration into two major fractions (MPH-1 <3 kDa, MPH-2 >3 kDa). Fraction MPH-1, which exhibited the highest antioxidant activity, was further fractionated by gel column into three fractions (MPH-1A, MPH-1B, and MPH-1C). The antioxidant activity of the MPH-1B fraction was stronger than that of the other fractions. Eight mungbean peptides (P1-P8) were identified in fraction MPH-1B by UPLC-Q-TOF-MS. Among them, peptides Trp-Gly-Asn (WGN, P2), Ala-Trp (AW, P4), Arg-Gly-Trp-Tyr-Glu (RGWYE, P5), and Gly-Val-Pro-Phe-Trp (GVPFW, P7) had high antioxidant activity. Moreover, these four peptides exerted protective effects against H2 O2 -induced cytotoxicity and regulated the MDA content, CAT activity, and total GSH content in HepG2 cells with specific observation. This study demonstrated the potential of MPH as a source of antioxidant peptides. This provides a scientific basis for the preparation of antioxidant peptides from mungbean protein. PRACTICAL APPLICATION: This study demonstrated the potential of the hydrolysate of mungbean protein as a source of antioxidant peptides and provided a scientific basis for the preparation of antioxidant peptides from mungbean protein.
Keywords: HepG2 cell; antioxidant peptide; cytoprotective effect; identification; mungbean protein; purification.
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