Preparation and identification of antioxidant peptides from cottonseed proteins

•Cottonseed peptides are prepared by enzymatic hydrolysis and microbial fermentation.•Cottonseed peptides show free radical scavenging and ferrous ion chelating activity.•Cottonseed protein hydrolysates are rich in acidic/basic and aromatic amino acids.•Cottonseed peptide YSNQNGRF has the potential as inhibitor of Keap1-Nrf2 interaction. The objective of this study was to investigate the antioxidant properties of cottonseed peptides. Results indicated that cottonseed peptides prepared by enzymatic hydrolysis and microbial fermentation both showed antioxidant properties. The cottonseed protein enzymatic hydrolysate with molecular weight less than 3 kDa exhibited excellent DPPH, ABTS and hydroxyl radical scavenging activity and ferrous ion chelating activity with EC50 values of 0.49 ± 0.02, 2.05 ± 0.02, 2.21 ± 0.12, and 0.99 ± 0.03 mg/mL, respectively. Amino acid composition analysis revealed that cottonseed protein hydrolysates are rich in acidic/basic and aromatic amino acids. In addition, among the 19 identified cottonseed protein-derived peptides, YSNQNGRF had the lowest CDOCKER energy and formed hydrogen bonds with Tyr334, Arg380, Arg415, Ser508, and Ser602, and van der Waals interactions with Asn382, Tyr525, Gln530, and Ser555, which all located in the binding site of Keap1-Nrf2 interaction. These findings suggested that the antioxidant peptides from cottonseed protein had the potential as functional ingredients in foods.