4.7 Article

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

Journal

FOOD CHEMISTRY
Volume 175, Issue -, Pages 258-266

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2014.11.142

Keywords

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

Funding

  1. Key Projects in the National Science & Technology Pillar Program during the Twelfth Five-Year Plan Period [2012BAD33B03]
  2. Jilin University [2014070]

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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 60 mM, respectively. Thus, the three peptides may have potential applications as a functional food, which could also be used as nutraceutical compounds. (c) 2014 Elsevier Ltd. All rights reserved.

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