A　series　of　diluted　and　concentrated　wheat　gluten　solutions　were　used　in　this　experiment　to　carry　out　deamidation　under　moist　heat.　During　the　moist-heat-induced　denaturation,　the　effect　of　molecular　structure　and　aggregation　state　of　wheat　gluten　on　the　degree　of　deamidation　was　analyzed.　The　results　showed　that　the　degree　of　deamidation,　degree　of　hydrolysis,　and　zeta　potential　significantly　decreased　with　increasing　aggregation　of　native　wheat　gluten.　Additionally,　both　degree　of　deamidation　and　hydrolysis　had　a　good　linear　relationship　with　the　changes　in　the　aggregation　state　of　wheat　gluten.　The　intermolecular　force　of　wheat　gluten　significantly　increased　with　increasing　aggregation　of　native　wheat　gluten,　and　the　red　shift　became　smaller.　The　intermolecular　noncovalent　bonds,　including　hydrogen　bonding　and　hydrophobic　interaction,　were　the　main　molecular　forces　for　the　aggregated　wheat　gluten;　disulfide　bonds　had　a　minimal　effect.　These　results　demonstrated　that　the　aggregation　state　of　native　wheat　gluten　is　closely　related　to　the　rate　of　wheat　gluten　deamidation　via　moist　heat　treatment　using　food-grade　organic　acid.　The　aggregation　state　of　native　wheat　gluten　is　the　most　important　factor　for　the　unfolding　degree　of　protein　molecules　and　aggregation　trends　of　wheat　gluten.　©　2015,　South　China　University　of　Technology.　All　right　reserved.