Effect of β-Ovomucin on the Solubility of α-Ovomucin and Further Inspection of the Structure of Ovomucin Complex in Thick Egg White

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-ovomucinwas 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. β-Ovomucin inhibited the formation of an insoluble α-ovomucin complex with lysozyme in neutral or slightly alkaline pH regions.
It was presumed that bound β-ovomucin inhibits the aggregation of the α-ovomucin-lysozyme complex in thick egg white and results in the formation of a gel structure.