Novel bioactive peptides with dual antioxidant and uric acid-lowering activities identified for the first time from Xanthoceras Sorbifolium Bunge seed meal: molecular docking and in vitro activity evaluation

The development of bioactive peptides from natural plant sources into functional foods and immunomodulatory is becoming an attractive approach. Seed meal protein is a high-quality plant protein that has shown potential as a source of bioactive peptides. In this study, the bioactive peptide from Xanthoceras Sorbifolium Bunge seed meal (XSBS) was obtained for the first time using ultrasound-assisted enzymatic hydrolysis. The molecular mechanisms underlying the bioactivity of XSPs have been explored by in silico and in vitro activity evaluation. The results of the study indicate that XSPs-I exhibits the highest ABTS radical scavenging rate (IC 50 =2.041 mg/mL), while XSPs-II demonstrates the highest DPPH radical scavenging rate (IC 50 =0.072 mg/mL) and the highest XOD inhibition rate (IC 50 =1.010 mg/mL). By further identifying and virtual screening of a large number of peptides of different XSPs, we have discovered that YPCCG exhibits binding energy with Keap1 and GLUT9. Finally, in vitro bioactivity evaluations of selected target peptides indicated that the peptide Tyr-Pro-Cys-Cys-Gly (YPCCG) possesses dual antioxidant and uric acid-lowering activities. These findings suggest that peptides derived from XSBS have significant potential for use as functional food ingredients. Concurrently, these findings provide new insights into the potential nutritional value of these peptides and their future applications. • Bioactive peptides were first prepared from Xanthoceras sorbifolium Bunge seed meal. • The antioxidant and uric acid-lowering activities were concurrently investigated. • YPCCG is a peptide that exhibits both antioxidant and uric acid-lowering activities.