ovalbumine

Ovalbumin, also referred to as ovalbumine, is the principal protein found in egg white (the albumen) of chickens and many birds. It accounts for about half of the total egg white protein and is a water-soluble glycoprotein. The mature molecule contains roughly 385 amino acids and a molecular weight of about 45 kilodaltons. It is synthesized in the oviduct and secreted into the forming egg, where it serves as a nutrient reservoir and contributes to the viscosity and buffering capacity of the albumen.

Biochemically, ovalbumin is a relatively stable protein with a structure that includes disulfide bonds and glycosylation sites. It is soluble in water and undergoes denaturation and gelation upon heating, a property exploited in food processing. Its thermal stability is lower than that of some other egg white proteins, such as ovomucoid, but it remains a widely studied model protein in folding and stability research.

Ovalbumin is one of the major egg white allergens in humans. In allergen databases it is listed as Gal d 2. Sensitization can lead to IgE-mediated reactions, and the clinical response can vary with heating, pH, and digestion because ovalbumin is relatively heat-labile compared with some other egg white allergens.

In research and industry, ovalbumin is used as a standard protein substrate in biochemistry, a model protein for studying protein folding and stability, and as a component in food products affecting texture and gelation. It is also used as an antigen in immunological assays and allergenicity studies.