Interaction between Ovalbumin andκ- orβ-Casein Due to Heating

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Abstract
The interactions between ovalbumin and .kappa.- or .beta.-casein due to heat-treatment of the mixtures were examined. The interaction between ovalbumin and .kappa.-casein was confirmed by the viscosity change of the mixture, the change in denaturation level of ovalbumin and the change in the ability of .kappa.-casein to stabilize Ca-.alpha.s-caseinate. Contribution of electrostatic bindings to the interaction was partly confirmed by acetylation of the proteins. The reaction through SH groups of denatured ovalbumin and .kappa.-casein was not responsible for the interaction. The interaction between ovalbumin and .beta.-casein was recognizable even at 25.degree. C. This interaction was evidenced not by the viscosity change but by the change of sound velocity in the mixture and the partial inhibition by .beta.-casein of the exposure of SH groups of ovalbumin when heated.

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