Purification and characterization of antioxidant peptides from enzymatic hydrolysate of mungbean protein.

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 H O -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.