Digestion differently affects the ability of native and thermally aggregated ovalbumin to trigger basophil activation.

Ovalbumin (OVA), a major allergen from hen's egg albumen, tends to aggregate when heated. Depending on the balance of attractive and repulsive interactions, heat-induced OVA aggregates have various morphologies, which differ in digestibility. In the context of food allergy to egg, we investigated the ability of native and thermally aggregated OVA as well as their digests to induce the degranulation of a humanized rat basophil leukemia (RBL) cell line, which was sensitized with a pool of sera from egg-allergic children. Native and two thermally aggregated OVA forms were digested in vitro using a gastrointestinal digestion model based on the INFOGEST harmonized protocol including a final degradation with jejunal brush border membranes (BBM) enzymes. The course of digestion was monitored by the OPA method and by RP-HPLC. Digestibility was OVA small aggregates>OVA large aggregates>>native OVA and BBM peptidases only significantly hydrolyzed small-sized peptides from gastro-duodenal digests of the aggregates. The degranulation ability of the native OVA slightly changed during the gastric phase but mostly decreased during the duodenal digestion with no further change with BBM digestion. The degranulation ability of aggregates, which was significantly lower than the ability of native OVA, was not significantly affected by digestion. Digestibility and ability to induce basophil degranulation can thus not be straightforward linked.