Changes in wheat kernel proteins induced by microwave treatment

• Wheat kernels were subject to a microwave treatment to reach high temperature for a short time.
• Proteins polymerized forming intermolecular bonding between the same class of proteins.
• Gliadins from treated flours reduced significantly their cross-reactivity with the R5 antibody.
• Gluten from treated flours become soluble in aqueous saline solution.
• Treated flours, in presence of water, were able to form dough, leavened and give rise to bread.

Wheat kernels were subjected to microwave treatment, and the proteins were characterized by size exclusion high-performance liquid chromatography (SE-HPLC) and sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE). Using this process, the proteins polymerize, forming intermolecular bonds among the same classes of proteins. Furthermore, the polymerization occurs only through disulphide bonds. Although SDS–PAGE did not show any differences for either the number or intensity of protein bands between flour samples before and after microwave treatment, gliadins from treated flours showed significantly reduced cross-reactivity with the R5 antibody. Moreover, the gluten became soluble in an aqueous saline solution, and it was not possible to isolate it using the Glutomatic apparatus. However, the treated flour, in the presence of water, was able to form dough and leaven and produce bread.