Why does denaturation of albumen protein cause pH of solution to increase?
The main component of egg white, ovalbumin, contains 93 negatively charged residues (Asp + Glu) and 68 positively charged residues (Arg + Lys), as well as 14 His. If you make the solvent less polar by adding ethanol to water, they will tend to form the neutral species (Arg+ and Lys+ will lose a proton, and Glu- and Asp- will pick up a proton).
If you had the protein unfolded already, you would expect that the solution gets more basic if the effect on all charged amino acids is the same because there are more negatively charged ones.
To test whether the observed effect has to do with denaturation of the proteins or with changes in protonation state of side chains already exposed to water, you could measure the pH of amino acids (preferably with a modification of the main chain carboxylic acid and amino functions so only the side chains show acid/base reactions) at different ethanol concentrations.