Use of dielectric properties to detect egg protein denaturation.
Changes in water and ion binding that occur during egg protein denaturation can be detected by measuring the dielectric properties. The dielectric properties of egg yolk, egg white and egg ovalbumin were tested from 25 to 105 degrees C at 11 frequencies from 300-2450 MHz. DSC was used to determine the temperature of protein denaturation. Both the dielectric constant and loss factor of egg yolk decreased due to denaturation of the protein lipovitellin. The dielectric constant increased at the initial denaturation and decreased after the complete denaturation and aggregation of egg ovalbumin in both egg white and ovalbumin.
Bircan
C
C
Department of Food Science and Technology, Ohio State University, Columbus, OH, USA.
Barringer
S A
SA
D002152:Calorimetry, Differential Scanning; D015387:Egg Proteins, Dietary / Q000528:radiation effects*; D004530:Egg Yolk; D004553:Electric Conductivity; D004574:Electromagnetic Fields; D010047:Ovalbumin / Q000737:chemistry; D011489:Protein Denaturation / Q000528:radiation effects
D015387:Egg Proteins, Dietary; D010047:Ovalbumin