Heating of an Ovalbumin Solution at Neutral pH and High Temperature.

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  • PHOTCHANACHAI Songsin
    <i>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University</i>
  • MEHTA Alka
    <i>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University</i>
  • KITABATAKE Naofumi
    <i>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University</i>

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  The thermal denaturation, aggregation, and degradation of hen egg white ovalbumin dissolved in distilled and deionized water (60 mg/ml, pH 7.5) was investigated by differential scanning calorimetry (DSC), polyacrylamide gel electrophoresis (PAGE), and viscosity measurement. Two independent endothermic peaks were observed up to 180°C by the DSC analysis. The first peak appeared at around 80°C, corresponding to the denaturation temperature of ovalbumin. The second peak occurred around 140°C due to the degradation of protein molecules as judged from the analysis by SDS-PAGE. The viscosity of the ovalbumin solution increased dramatically above 88°C and maintained almost the same value up until heating to 140°C. The increase in viscosity after heating to 88°C was due to the denaturation and subsequent aggregation of ovalbumin molecules as observed by SDS-PAGE. The decrease in viscosity of the samples heated above 150°C appears to have been the result of degradation of the ovalbumin molecules.<br>

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