Structural Variations of Wheat Proteins under ultrasound treatment

The present work investigated the effects of ultrasound on hydrogen-bond strength, secondary and network structures, granule size microstructures gluten, glutenin gliadin, in order to explicate possible mechanisms ultrasound-assisted dough processing. results showed that weakened intermolecular strength protein. After sonication, contents ?-turns ?-sheets decreased increased, respectively, which was especially evident under medium-intensity sonication (23.08 W/L; 30 min) among low-, medium- high-intensity. This implied ultrasonic treatment facilitated conversion into ?-sheets. Sonicated gluten proteins have uniform sizes exhibit a flocculent, rough, fluffy relatively dispersed structure with loosely distributed particles. has complete more ordered crosslinks between molecules. For sonicated small pores can be observed surface its overall appears enlarged. Generally, could affect protein by hydrogen-bonding interactions, as well molecular crosslink, distribution, mechanical properties air chamber structure.