The aggregation between lysozyme and heat-denatured ovalbumin was investigated by measuring the development of turbidity. The obtained aggregates were found to consist of lysozyme and ovalbumin at the molar ratio of 1.5, from the result of electrophoretic analysis. The aggregation was inhibited by the addition ofNaCl or the acylation oflysozyme. This result suggests that the lysine residues in lysozyme were directly involved in the aggregation process. It is suggested that the cysteine residues in ovalbumin did not participate in the aggregation with lysozyme. The degree of aggregation reached its maximumwhenthe ovalbumin solution was heated to 75°C, and was suppressed by the association of ovalbumin molecules during heat denaturation. From these results, it was found that lysozyme interacted electrostatically with the monomeric molecule of fully unfolded ovalbumin during aggregation. Egg white is extensively utilized as a functional food material in food processing. Heat coagulation is one of the important functional properties of egg white; therefore, the coagulation of egg white protein has been extensively studied by many investigators.1~8) However, heat-induced interaction among the hetero
The heat-induced aggregation between ovalbumin and lysozyme was investigated under various conditions by measuring the development of turbidity. The result of sodium dodecylsulfatepolyacrylamide gel electrophoresis in the presence of 2-mercaptoethanol indicated that the obtained aggregate consisted of nearly the same amounts of ovalbumin and lysozyme. The heat-induced aggregation was inhibited by an increase of ionic strength. The effect of chemical modifications (succinylation and carboxymethylation) of the proteins on the heat-induced aggregation was examined to estimate the participation of specific amino acid residues in the aggregation process, the result indicating that the lysine and cysteine residues in the proteins were directly involved. From these results, it is suggested that the heat-induced aggregation between ovalbumin and lysozyme is due to an electrostatic attraction and sulfhydryl-disulfide interchange between the heatdenatured protein molecules. Egg white is extensively utilized as a functional food material in food processing. Heat coagulability is one of important functional properties of egg white; therefore, the heat denaturation of egg white and its component proteins has been studied by many investigators.1~8) However, heat-induced interaction among the heterogeneous proteins in egg white has been little studied. It has been reported9'10* that ovalbumin and lysozyme,
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