Casein: allergenicity and molecular properties

Caseins represent about 80% of total protein in cow’s milk. Individual caseins, αs1, αs2, β and κ-casein, are characterized by specific structure and function. Besides their role in cheese-making, casein subunits exhibit molecular properties and structure which confer them technological and functional properties exploited in food and pharmaceutical industries for a long time. Nutrititional value and beneficial effects due the release of bioactive peptides are also widely reported. Despite their valuable properties, caseins are able to trigger even severe immuno reactions in sensitive individuals thus representing one of the most important allergenic source in the food allergens landscape. The exploitation of high throughput technologies combined with advanced bioinformatic tools promotes advanced research directed to identify and characterize new epitopes capable of inducing an onset of allergic reaction in predisposed consumers. On the other hand, several efforts are underway to develop innovative solutions to reduce caseins allergy by preserving nutritional quality of proteins. The chapter aims to give a broad overview on the main proteins constituting cow’s milk, the related molecular properties as well as to provide some knowout about their functioning properties in food processing. The focus is then moved forward to allergenic properties of caseins and capability of milk proteins to trigger cow’s milk allergy (CMA) in sensitive consumers. Processing strategies to mitigate casein allergenicity and CMA prevention, management and therapeutic approaches are also presented.