Isolation, Purification And Structural Identification Of Antioxidant Peptides From Soybean Oligopeptides
Keywords
Abstract
Abstract In order to investigate the activity and structure of antioxidant peptides in soybean oligopeptides, soybean oligopeptides were prepared using soybean protein isolate as raw material and a two-step enzymatic hydrolysis method. Based on the analysis of its physical and chemical components, DPPH free radicals were used to The scavenging ability was used as an index to evaluate its antioxidant activity. The results showed that the IC50 value of the DPPH free radical scavenging activity of soybean oligopeptides was about 2.6 mg/mL. Reversed-phase high-performance liquid chromatography (RP-HPLC) was used to analyze soybean oligopeptides. The oligopeptides were separated and purified, six component peaks were collected, and their DPPH free radical scavenging abilities were measured. The results showed that the activities of the six components were higher than those of soybean oligopeptides. Finally, a Q-TOF mass spectrometer was used to measure The structure of the most active component 5# was identified, and the DPPH free radical scavenging activity of the six identified peptides was evaluated. The results showed that all six peptides had a certain DPPH free radical scavenging ability, among which Leu -Tyr(LY), Leu-Ala-Gly-Arg(LAGR), and Phe-Ser-Arg(FSR) have higher clearance rates than soy oligopeptides and are peptides with high antioxidant activity
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