Structural and proteomic characteristics of the extracted protein from thermal sterilized soy seeds and their effects on IgE reactivity, antioxidant activity and interfacial properties

The study assessed protein structural and proteomic characteristics from thermal-sterilized (boiling and autoclaving) soy seeds and their effects on allergenicity, antioxidant activity and interfacial properties. Results demonstrated that boiling and autoclaving caused protein degradation and a reduction of soluble protein content and particle size. Scanning electron microscopy, Fourier transform infrared, ultraviolet and fluorescence spectroscopy showed that autoclaving is more effective than boiling in causing protein aggregation and secondary and tertiary structural changes. Proteomic analysis using LC/MS-MS revealed that autoclaving caused more changes of protein composition than boiling, with lower contents of major allergenic proteins and less reduction in linear epitopes. Thus, the autoclaved samples exhibited more reduction (81.5 %) of IgE reactivity than boiled samples (43.5 %). Additionally, autoclaving increased antioxidant activity more than boiling but caused a greater reduction in interfacial foaming and emulsifying) properties. This study provides a foundation for producing hypo-allergenicity soy products through industry sterilization techniques.