Effects of decolorization on aggregation behavior of highland barley proteins: Comparison with wheat proteins.

To explore effects of decoloration on highland barley proteins (HBPs) aggregation, physicochemicalproperties, structuralcharacteristics, and functional characteristics of decolorized highland barley proteins (DHBPs) were investigated. In order to compare the aggregation of HBPs, wheat proteins (WPs) were selected as a control group. The solubility, turbidity, particle size and surfacehydrophobicity of HBPs increased obviously (P < 0.05) after decoloration, but still lower than WPs. Electrophoretic analysis showed that the bands amount of HBPs and DHBPs were lower than WPs, while decolorization had no effect on the bands amount of HBPs. Moreover, chemical bonds contents of DHBPs were higher than HBPs, but significant lower (P < 0.05) than WPs. The Fourier-transform infrared spectroscope showed that secondary structures of HBPs were more flexible after decoloration. Besides, foaming property, emulsifying property and water holding capacity of DHBPs increased significantly (P < 0.05). To conclude, the aggregation behavior and functional properties of HBPs were improved by the decolorization.