This study sought to purify and identify antioxidant peptides from sheep (Ovis aries) plasma protein hydrolysates and assess their protective impacts on H2O2-induced Caco-2 cells. The purification process involved reversed high-performance liquid chromatography, anion-exchange chromatography, and Sephadex G-25. Three peptides, namely Trp-Glu-Glu-Pro-Ala-Met (WEEPAM), Ser-Leu-His-Phe-Met-Glu (SLHFME), and His-Cys-Thr-Thr-Phe-Met-Ile, with molecular weights of 761.84, 762.87, and 852.03 Da, respectively, were identified by liquid chromatography with tandem mass spectrometry. Among the three antioxidant peptides, superoxide radical (O2 -) radical scavenging capacity of WEEPAM and SLHFME was not significantly different from glutathione (GSH) (p > 0.05), while their 1,1-diphenyl-2-picrylhydrazyl radical scavenging capacity was greater than GSH (p < 0.05). WEEPAM revealed increased antioxidant activity after pepsin and trypsin hydrolysis under an in vitro digestion model. In addition, WEEPAM inhibited oxidative damage in Caco-2 cells by significantly reducing reactive oxygen species accumulation, early apoptosis, malondialdehyde formation, and increasing intracellular superoxide dismutase, glutathione peroxidase, and catalase activities.
Keywords: antioxidant peptide; cell protection; radical scavenging activity; sheep plasma protein.
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