Abstract
The aggregation behavior of gluten proteins via electrostatic interactions or hydrogen bonds during dough formation was investigated. Proteins were extracted with 50 mM acetic acid or 4 M urea to break electrostatic interactions or hydrogen bonds, respectively. The extracted proteins were analyzed by size exclusion high performance liquid chromatography and two dimensional fluorescence difference gel electrophoresis. Acetic acid- and urea-soluble protein aggregates increased with dough development, indicating that electrostatic interactions and hydrogen bonds weakened during dough mixing. On the other hand, the some monomeric proteins (mainly α-gliadins) in dough aggregated via electrostatic interactions rather than hydrogen bonds. A model is proposed for gluten formation during dough mixing based on non-covalent bonds.
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