Purification, Identification, and Mechanistic Investigation of Novel Selenium-Enriched Antioxidant Peptides from Moringa oleifera Seeds

In this study, five novel Se-enriched antioxidant peptides (FLSeML, LSeMAAL, LASeMMVL, SeMLLAA, and LSeMAL) were purified and identified from Se-enriched Moringa oleifera (M. oleifera) seed protein hydrolysate. The five peptides showed excellent cellular antioxidant activity, with respective EC50 values of 0.291, 0.383, 0.662, 0.1, and 0.123 mu g/mL. The five peptides (0.025 mg/mL) increased the cell viability from 78.72 to 90.71, 89.16, 93.92, 83.68, and 98.29%, respectively, effectively reducing reactive oxygen species accumulation and significantly increasing superoxide dismutase and catalase activities in damaged cells. Molecular docking results revealed that the five novel Se-enriched peptides interacted with the key amino acid of Keap1, thus directly blocking the interaction of Keap1-Nrf2 and activating the antioxidant stress response to enhance the ability of scavenging free radicals in vitro. In conclusion, Se-enriched M. oleifera seed peptides exhibited significant antioxidant activity and can be expected to find widespread use as a highly active natural functional food additive and ingredient.

Automated summary

In this study, five novel Se-enriched antioxidant peptides were extracted and identified from Se-enriched Moringa oleifera seed protein hydrolysate. These peptides exhibited excellent cellular antioxidant activity, effectively reducing reactive oxygen species accumulation and increasing superoxide dismutase and catalase activities in damaged cells. Moreover, these peptides interacted with the key amino acid of Keap1, blocking the interaction of Keap1-Nrf2 and activating the antioxidant stress response in vitro.