4.5 Article

Improvement of the solubility and emulsification of rice protein isolate by the pH shift treatment

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WILEY
DOI: 10.1111/ijfs.15834

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Emulsification; pH shift treatment; protein structure; rice protein isolate; solubility

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The study demonstrated that pH shift treatment significantly improved the solubility and emulsification of rice protein isolate under neutral conditions. The treatment led to decreased particle size, changes in protein structure, and enhanced emulsion stability. Overall, the method improved the structural and functional properties of the protein for food applications.
In the current research, we have adopted a pH shift treatment method that can significantly improve the solubility and emulsification of rice protein isolate (RPI) under neutral conditions. Our results showed that the RPI reached a quasi-equilibrium state at 1 h after alkali shift treatment, and the solubility and emulsifying properties of RPI were significantly improved compared with the control. In addition, the particle size of RPI decreased considerably under the alkali shift treatment. The results of electron microscopy showed that the RPI aggregates were depolymerised and the particle size distribution was more uniform. The pH shift treatment induced the rearrangement of protein secondary structure, and the exposure of hydrophobic groups increase the surface hydrophobicity of RPI. The change in endogenous fluorescence spectrum, UV and the disulfide bond content all showed that the conformation of RPI changed significantly through pH shift treatment. In addition, it was found that the RPI treated under pH 10-11 shift possessed the best property to stabilise the emulsion. This study showed that under the condition of pH10 and pH11 shift treatment, the structural and functional properties of RPI were vastly improved, and the application of RPI in food was greatly ameliorated.

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