Antioxidant peptides obtained from goose egg white proteins by enzymatic hydrolysis

Authors

  • Mohammad-Hossein Baratzadeh,

    1. Department of Biology, Faculty of Sciences, Mashhad Branch, Islamic Azad University, Mashhad, Iran
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  • Ahmad Asoodeh,

    Corresponding author
    1. Department of Chemistry, Faculty of Sciences, Ferdowsi University of Mashhad, Mashhad, Iran
    2. Cellular and Molecular Research Group, Institute of Biotechnology, Ferdowsi University of Mashhad, Mashhad, Iran
    • Department of Biology, Faculty of Sciences, Mashhad Branch, Islamic Azad University, Mashhad, Iran
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  • Jamshidkhan Chamani

    1. Department of Biology, Faculty of Sciences, Mashhad Branch, Islamic Azad University, Mashhad, Iran
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Correspondent: Fax: +98 511 8795457;

e-mail: asoodeh@um.ac.ir

Summary

In this study, antioxidant peptides from goose egg white proteins produced using various enzymes were purified and characterised. Two peptides were named as p14 and p16, showing the highest scavenging activity of 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical and the highest metal ion chelating activity, respectively. The sequences of p14 and p16 were identified to be STMMEERRMKVY (1560.72 Da) and DVFRELRVQ (1161.62 Da), respectively. The sequence of p14 has a similarity of 75% to ovalbumin from Meleagris gallopavo and the sequence of p16 has a similarity of 67% to ovalbumin from Taeniopygia guttata. IC50 values of p14 and p16 were determined, and results showed that DPPH radical scavenging activity was 81.6 and 205.5 μm, 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonicacid)(ABTS) radical scavenging was 88.4 and 153.8 μm, hydroxyl radical scavenging was 85.5 and 116.3 μm and metal ion chelating was 170.6 and 117.9 μm, respectively. The two identified peptides from goose egg white hydrolysates act as potent natural antioxidant agents.

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