Insights into Isolation and Purification Strategies of Egg Allergens

Eggs are a great source of protein in the human diet. They are consumed in tens of millions of tons globally per year. In addition, egg proteins, which are known food allergens, are included in many food products due to their excellent techno-functional properties. Hen’s eggs are the most consumed, but other edible avian eggs are occasionally used as gourmet ingredients or delicacies. With a high presence in the food market, the risk of accidental exposure to egg allergens is high. Hen egg allergy ranks among the top three food allergens in infants and young children. The complex structure and similar physicochemical properties of egg proteins limit their separation and purification, making further research challenging. Egg composition is influenced by age, disease, medicine, and environmental stress, and the target protein is often present in negligible amounts or polymorphic forms. To investigate the immunoreactivity of proteins from eggs of different bird species, it is necessary to consistently and quantitatively extract and purify proteins while avoiding harsh conditions. The conformational shape of allergens is impacted by denaturation, which can remove or expose IgE-binding epitopes and change the allergenic potential of proteins. This review presents findings from a literature survey on the isolation and purification strategies utilized for egg allergens from culinary-relevant bird eggs.