摘要
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 cm(3)/g) than the control wheat bread (4.52 cm(3)/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.
- 出版日期2010-9