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Abstract
The effect of β -ovomucin on the solubility of α-ovomucin was studied in the presence or absence of lysozyme. The α -ovomucin content in a mixed solution of α-ovomucin was calculated with a simultaneous equation devised on the basis of the differences in the protein and carbohydrate contents of the two ovomucin.
β -Ovomucin inhibited the formation of α -ovomucin aggregates in a salt-free solution or in a slightly acid one. α -Ovomucin formed an insoluble complex with lysozyme below pH 10 at the ionic strength of 0.01, and β-ovomucin formed an insoluble complex with lysozyme below pH 6. ß - Ovomucin inhibited the formation of an insoluble α -ovomucin complex with lysozyme in neutral or slightly alkaline pH regions.
It was presumed that bound ß -ovomucin inhibits the aggregation of the α-ovomucin-lysozyme complex in thick egg white and results in the formation of a gel structure.