After　carboxylic　acid　deamidation　upon　heating　(CADH),　wheat　gluten　still　contains　a　total　of　similar　to　10%　insoluble　fractions,　of　which　similar　to　10%　is　starch,　which　depreciate　the　values　of　wheat　gluten.　To　elucidate　gluten-starch　interactions　and　their　role　in　the　deamidation　behavior　of　gluten,　the　macrostructural　characteristics　of　gluten　citric　acid　suspensions　of　different　concentrations　(1%　and　10%,　w/v)　and　with　different　types　of　residual　starch　chains　(achieved　by　enzyme　hydrolyzed　by　a-amylase　and/or　glucoamylase　assisted　by　sonication)　were　investigated.　We　found　the　degradation　of　long　starch　chains　and　branched　short　chains　induced　dramatic　bond-cleavages　in　insoluble　glutenins　and　gliadins.　FTIR　and　SDS-PAGE　analyses　indicated　that　without　these　two　types　of　chains　in　the　precipitates,　the　insoluble　deamidated　wheat　gluten　exhibited　minimal　changes　in　the　molecular　force　and　the　conformation.　Their　glycosylation,　hydrophobic　force　and　hydrogen　bonds　between　amylopectin　and　small　proteins,　such　as　LMW-GS　and　alpha,　beta,　gamma-gliadins,　were　detected.　FTIR　suggested　that　the　associations　between　gliadins　and　amylopectin　were　covalent.　Gluten-starch　interactions　were　likely　to　cause　an　incomplete　dissolution　of　wheat　gluten　during　CADH.　A　simple　model　was　proposed　to　clarify　the　aggregation　state　and　the　relationships　between　starch　granules　and　wheat　gluten　components　during　CADH.