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The way in which proteins aggregate when heated may change their sensitising potency

Food allergies affect 5% of adults and 8% of children and their frequency is increasing.

Determining the best form in which a food should be consumed to limit allergic sensitisation is a public health issue. Thermal treatments are known to alter the triggering ability of allergens and many egg-allergic children tolerate eggs in cakes/biscuits. In this study, we showed that the way in which ovalbumin (the major egg white protein) aggregates during heating also modulates its sensitising capacity.

Food allergy to egg white is common in young children: in Europe, it affects 1% of children under two years of age and up to 2% in Northwestern Europe

Egg white is consumed in many forms whose sensitizing capacities are unknown. Ovalbumin constitutes more than 50% of the proteins in egg white. Depending on the physico-chemical conditions, heating ovalbumin leads to the formation of aggregates that vary in size and in morphology. Small (5-80 x 10-9m) and large (3-300 x 10-6m) ovalbumin aggregates were produced by heating the protein under opposite physico-chemical conditions to compare the sensitising capacity of these aggregates and that of the native protein using a mouse model.


Claude, M., Lupi, R., Bouchaud, G., Bodinier, M., Brossard, C., & Denery-Papini, S. (2016). The thermal aggregation of ovalbumin as large particles decreases its allergenicity for egg allergic patients and in a murine model. Food Chemistry, 203, 136–144.

Claude, M., Bouchaud, G., Lupi, R., Castan, L., Tranquet, O., Denery-Papini, S., Bodinier M., Brossard, C. (2017). How protein aggregates can reduce allergenicity: comparison of ovalbumin heated under opposite electrostatic conditions. Journal of Agricultural and Food Chemistry, 65 (18), pp 3693–3701.