Effect of Ultrasonic on the Structure of Wheat Gluten Protein

【Objective】 The information on the gluten protein structure alterations affected by ultrasonic would provide a theoretical basis for the changes of functional properties under ultrasonic. 【Method】 The secondary structure, inner/intra molecules interaction as well as micro structure of gluten after ultrasonic treatment were studied by using FTIR, SEM and laser particle mastersier 2000. 【Result】 The β-turn percentage of gluten protein significantly decreased while the α-helix percentage increased after ultrasonic under all power levels, but the β-sheet percentage altered as the ultrasonic power level differed. In addition, the SS bond, hydrogen bond and hydrophobic bond among inter/intra molecules were destroyed, which resulted in the formation of incompact structure shown by SEM and indicated by the increase of volume particle size of gluten protein. 【Conclusion】 Ultrasonic reduced the inner/intra molecules interaction among gluten molecules, whereby the incompact structure formed.