Food Science of Animal Resources (한국축산식품학회지)

Korean Society for Food Science of Animal Resources (한국축산식품학회)
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Purification and Characterization of an Antioxidant Protein from Fertilized Eggs

  • Yang, Shaohua (College of Biotechnology and Food Engineering, Hefei University of Technology) ;
  • Tang, Zhengjiang (College of Biotechnology and Food Engineering, Hefei University of Technology) ;
  • Tang, ShanShan (College of Biotechnology and Food Engineering, Hefei University of Technology) ;
  • Zhang, Tingfang (College of Biotechnology and Food Engineering, Hefei University of Technology) ;
  • Tang, Fei (College of Biotechnology and Food Engineering, Hefei University of Technology) ;
  • Wu, Yu (College of Biotechnology and Food Engineering, Hefei University of Technology) ;
  • Wang, Ying (College of Biotechnology and Food Engineering, Hefei University of Technology) ;
  • Wang, Lu Lu (College of Biotechnology and Food Engineering, Hefei University of Technology) ;
  • Liu, Guoqing (College of Biotechnology and Food Engineering, Hefei University of Technology)
  • Received : 2016.07.05
  • Accepted : 2016.11.25
  • Published : 2016.12.31
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Abstract

Free radicals may attack cells or tissue, leading to chronic diseases, and antioxidant consumption is potentially useful for removing free radicals. Egg proteins may be used as potential sources of antioxidant considering their ability of scavenging free radicals to apply for food or cosmetics industry. In this study, we obtained a natural antioxidant protein from fertilized eggs, which was a dietary supplement in some Asian countries. Meanwhile, antioxidant activities of these proteins were evaluated using different oxidation systems. With increasing incubation time, the antioxidant activity of these proteins increased during 15 d of incubation. The samples on day 15 were performed for isolation of antioxidant protein. The protein, named P4-1 (MW, 45 kDa), was isolated and purified by consecutive chromatographic methods. P4-1 contained 17 amino acids, which was determined by liquid chromatography-mass spectrometry and Amino Acid Analyzer. Moreover, the amino acid sequence was highly similar to that of ovalbumin. Differential scanning calorimetry showed that the denaturation temperature of P4-1 was $57.16^{\circ}C$. Furthermore, P4-1 suggested high oxygen radical-absorbance activity in ${\cdot}OH$ assays, and its antioxidant activity was stable at $30-50^{\circ}C$ in acidic and neutral pH. Thus, these results revealed that P4-1 may be a potential resource as a natural antioxidant.

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References

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