Electron beam irradiation induced aggregation, structural and functional changes of soybean 11S globulin.

Abstract

This study investigated the effects of different irradiation doses of an electron beam (e-beam) (0, 2, 4, 6, 8, and 10 kGy) on the structure, emulsification, foaming, and rheological and gel properties of soybean 11S globulin. The irradiation treatment at 4 and 6 kGy significantly increased the solubility, surface hydrophobicity, disulfide bonding, and ζ-potential of 11S globulin, decreased the particle size of the protein solution, and effectively improved the emulsifying activity and foaming stability of the protein solution. Moreover, irradiation induced moderate cross-linking and aggregation of the proteins, thereby increasing the apparent viscosity and shear stress of the protein solution. In addition, the low-field NMR and microstructure analysis results revealed that protein gels formed a dense and homogeneous three-dimensional mesh structure after irradiation (6 kGy), along with increased content of bound water (T_2b) and water not readily flowable (T₂₁) and a decrease content of free water (T₂₂). Overall, our results confirmed that e-beam irradiation could significantly improve the physicochemical properties of soybean 11S globulin. Our study thus provides a new technical means for the application of electron beam irradiation technology toward protein modification and broadens the high-value utilization of soybean 11S globulin in the food processing industry.