Ovalbumin is the predominant protein in avian egg white, constituting approximately 54% of total egg white protein. It is a phosphoglycoprotein with a molecular weight of about 45 kDa, consisting of 385 amino acid residues and containing N-linked glycosylation and phosphorylation sites. Ovalbumin serves as a storage protein providing amino acids for the developing embryo. In food science, it is valued for its foaming, emulsifying, and gelling properties, making it essential in baking, meringues, and confectionery. It denatures upon heating above 80°C, leading to coagulation. As a major food allergen, it is designated Gal d 2. Its structure includes four disulfide bonds and a reactive serine protease inhibitor-like fold, though it lacks inhibitory activity.