Wheat　gluten　was　deamidated　by　citric　acid　at　121　℃　for　2,　4,　6,　8　min.　The　change　of　structure　and　state　of　its　aggregative　behavior　controlled　by　the　concentration　of　protein　(from　dilute　to　sub-concentrated,　0.01-10　mg/mL)　and　deamidation　time　upon　the　process　of　deamidation　was　investigated.　Results　demonstrated　that　degree　of　deamidation　and　hydrolysis　enhanced　with　increasing　of　deamidated　time　and　decreased　with　the　lowering　of　original　aggregative　state.　Surface　hydrophobicity　of　deamidated　wheat　gluten　decreased　with　as　the　reducing　of　its　original　aggregative　state,　but　raised　up　with　deamidated　time.　Furthermore,　it　prompted　the　content　of　α-helix　decreased　and　shifted　to　β-turn　and　β-sheet　as　prolonging　the　processing　deamidation　time　and/or　reducing　original　aggregative　state　of　wheat　gluten.　Results　from　Zeta　potential,　SDS-PAGE,　FTIR　and　endogenous　fluorescence　demonstrated　that　original　aggregative　state　of　wheat　gluten　had　significantly　impact　on　unfolding　of　protein　structure　and　the　accessibility　of　H+　to　amide　groups　and　peptide　bonds.　Furthermore,　hydrogen　ions　from　citric　acid　was　susceptible　to　high　molecular　weight　glutenin　subunits　during　deamidation.　©　2018,　Editorial　Office　of　Journal　of　CIFST.　All　right　reserved.