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

• Published in: Journal of cereal science Vol. 52; no. 2; pp. 310 - 313
• Main Authors: CABRERA-CHAVEZ, Francisco, ISLAS-RUBIO, Alma R, ROUZAUD-SANDEZ, Ofelia, SOTELO-CRUZ, Norberto, CALDERON DE LA BARCA, Ana M
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier Ltd 01-09-2010; Elsevier
• Subjects: Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts; Biological and medical sciences; Bread making; Celiac disease; Cereal and baking product industries; Food industries; Fundamental and applied biological sciences. Psychology; Gluten modification; Immunoreactivity; Celiac disease; Bread making; CD; RH; Gluten modification; Immunoreactivity; ELISA; Modification; Aminoacid; Methionine; Wheat bread; Plant protein; Coeliac disease; Gluten; Soft wheat
• ISSN: 0733-5210; 1095-9963
• DOI: 10.1016/j.jcs.2010.06.013

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.