The fate of bioaccessible coeliac toxic motifs and IgE epitopes during simulated gastro-intestinal digestion of pizza base

ABSTRACT: Understanding how food processing may modify allergen bioaccessibility and the evolution of immunologically active peptides in the gastrointestinal tract is essential if knowledge-based ap-proaches to reducing the allergenicity of food is to be realised. A soy-enriched wheat-based pizza base was subjected to in vitro oral-gastro-duodenal digestion and resulting digests analysed using a combination of SDS-PAGE and mass spectrometry (MS). The digestion profile of pizza base resembled that of bread crust where higher temperatures during baking reduced protein solu-bility but still resulted in the generation of a complex mixture of peptides. MS profiling showed of the peptides carried IgE-epitopes and coeliac toxic motifs many of which were in excess of 20-30 residues long which were only released after extended (120 min) gastric digestion or a combina-tion of gastric and duodenal digestion. Comparison with in silico prediction tools showed that they either under-estimated pepsinolysis products or over estimated tryptic/chymotryptic cleavage patterns. These data show that simple thermal treatments, such as baking, are insuffi-cient to destroy the allergenic potential of wheat and soybean proteins. The findings contribute to efforts to provide bench marks for mapping in vitro digestion products of novel proteins as part of the allergenicity risk assessment.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Triticum Aestivum (wheat) Glycine Max

SUBMITTER: Matthew Daly  

LAB HEAD: Clare Mills

PROVIDER: PXD031067 | Pride | 2022-08-12

REPOSITORIES: Pride