Modification of gluten by methionine binding to prepare wheat bread with reduced reactivity to serum IgA of celiac disease patients

Celiac disease (CD) is caused by ingestion of wheat gluten proteins, due to immune response to proline- and glutamine-rich sequences. In this study, for reduction of the immune recognition, gluten proteins were enzymatically modified by binding methionine to the amino lateral groups of glutamine residues. Additionally, a bread-making process with modified gluten was assayed. The methionine binding was monitored by measuring the alpha-amino group disappearance and reduction of celiac IgA immunoreactivity. The best methionine binding was after 60 min reaction at pH 10, inducing a reduced to null IgA immunoreactivity to prolamins extracted from modified gluten. The bread prepared with modified gluten had lower specific volume (3.86 cm3/g) than the control wheat bread (4.52 cm3/g) but higher than those reported for gluten-free loaves. The preserved functionality of gluten proteins will make it feasible to apply this kind of modification in different wheat-based foodstuffs like the assayed bread in this study.