Dielectric Spectroscopy of Ovalbumin Under Different Temperatures

Serin M., Yakut Ş., Çalışkan M., Ulutaş H. K., Bozoğlu Parto D., Ulutaş D., ...More

Turkish Physical Society 35th International Physics Congress, Muğla, Turkey, 4 - 08 September 2019, vol.1, no.1, pp.336

  • Publication Type: Conference Paper / Summary Text
  • Volume: 1
  • City: Muğla
  • Country: Turkey
  • Page Numbers: pp.336
  • Yıldız Technical University Affiliated: Yes


The ovalbumin (abbreviated as OVA) is the main protein of white part of the egg, making up 55% of the total protein. Ovalbumin has sequence similarities and three-dimensional conformation with the superfamily of serpins, but unlike most serpins, it is not an inhibitor of serine proteases and  presumed to be a storage protein. The dielectrical behaviour of ovalbumin is unknown under AC electrical stress and temperatures. In this study, bulky ovalbumin structure were characterized by using broad band dielectric spectroscopy system Alpha-A which is high resolution Impedance Analyser. The dielectric spectroscopy of bulky ovalbumine samples were examined between the 0,1-2x107Hz frequency range.  The results showed that the dielectric constants and dielectric loss of the samples decrese with increasing frequency. On the other hand AC conductivity of the samples increase with increasing frequency having three different slope which are the evidence of the three different relaxation of the structure.