Re: How does Egg Albumen denature using ethanol?

A biochemistry text should be helpful on this. Briefly, most proteins, including albumen, are exposed to an aqueous environment (excepting those that are largely embedded in membranes). Thus, amino acids on the surfaces of the protein are compatible with the polar aqueous environment. In contrast, interior regions of proteins are often hydrophobic. Alcohol disrupts the hydrogen bonding between the water and the surface polar residues, favoring exposure of the more hydrophobic residues normally buried inside. This conformational change is referred to as denaturation.

That said, proteins are very heterogeneous, and each behaves somewhat differently. The principles outlined above are generally but not universally true. For a very nice discussion of the specific case of egg albumen, which is a mix of proteins, see: http://albumen.stanford.edu/library/c20/messier1991a.html