Purification and identification of novel antioxidant peptides from egg white protein and their antioxidant activities

Food Chem. 2015 May 15:175:258-66. doi: 10.1016/j.foodchem.2014.11.142. Epub 2014 Nov 29.

Abstract

The aim of this study was to isolate antioxidant peptides from egg white protein hydrolysates (EWPH) and identify novel antioxidant peptides by LC tandem mass spectrometric and mid-infrared spectroscopy (MIR). The amino acid composition of peptides was also analyzed by amino acid analyzer on the basis of ninhydrin reaction. Three novel peptides with molecular weights of 628.64 Da, 630.71 Da, and 684.1 Da were identified as Asp-His-Thr-Lys-Glu (DHTKE), Phe-Phe-Glu-Phe-His (FFGFN) and Met-Pro-Asp-Ala-His-Leu (MPDAHL), respectively. DHTKE exhibited the best oxygen radical absorbance capacity (P<0.05). The concentration of FFGFN and MPDAHL to scavenge 50% of DPPH radicals was 80 mM and 60mM, respectively. Thus, the three peptides may have potential applications as a functional food, which could also be used as nutraceutical compounds.

Keywords: Antioxidant peptide; Identification; Mid-infrared spectroscopy (MIR); Purification.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antioxidants / chemistry*
  • Antioxidants / isolation & purification
  • Egg Proteins / chemistry*
  • Oxidation-Reduction
  • Peptides / chemistry*
  • Peptides / isolation & purification
  • Spectrophotometry, Infrared / methods
  • Tandem Mass Spectrometry / methods

Substances

  • Antioxidants
  • Egg Proteins
  • Peptides