Isolation, Purification and Structural Identification of Aantioxidative Peptides from Egg White

In order to obtain high activity and high purity egg white antioxidant peptides, the egg white proteolytics were used as raw materials, and the peptides with strong antioxidant activity were separated and purified by ultrafiltration, ion exchange chromatography and gel chromatography. The amino acid sequence of the peptide chain was analyzed by matrix-assisted laser desorption ionization mass spectrometry. The results showed that the DPPH free radical scavenging rate of EWPH-III (MW<3 kDa) was up to 79.62% among the three components obtained by ultrafiltration separation and purification of EWPH. Among the two components obtained by ion exchange chromatography separation and purification of EWPH-III, the DPPH free radical scavenging rate of alkaline component B was up to 82.05%. The 4 components of EWPH-III-B were separated by gel filtration chromatography. The DPPH free radical scavenging rate of EWPH-III-B-E component was 88.49%. The relative molecular mass of EWPH-III-B-E was 237.575 and the amino acid sequence was Ala-Met.