Purification and Antioxidant Activity of Peptides Derived from Egg White Proteins

The peptides derived from egg white proteins were fractionated on Sephadex G-25 gel filtration column and the fraction with the highest DPPH· radical scavenging activity was purified on Sephadex G-15 gel filtration column. A total of 7 fractions were obtained by Sephadex G-25 gel filtration chromatography and fraction 3 showed the highest antioxidant activity with a DPPH· radical scavenging rate of 63.80% at 3 mg/ml. Fraction 3 was further separated into 4 subfractions,among which,subfraction 3-1 and 3-2 showed higher DPPH radical scavenging activities and the DPPH radical scavenging rates at 3 mg/ml were 84.02% and 81.17%,respectively. According to RP-HPLC chromatogram subfraction 3-1 had a high homogeneous composition.