Effects of pH-shifting treatments on the emulsifying properties of rice protein isolates: Quantitative analysis of interfacial protein layer.

For the limitation of poor solubility and interfacial adsorption capacity of rice protein isolates (RPI), in this work the effects of pH-shifting treatments on the emulsifying properties of RPI were investigated. The results showed that the particle size of the emulsion stabilized by alkaline pH-shifting treated RPI was smaller than that stabilized by acid pH-shifting treated RPI. In addition, the RPI-10 stabilized emulsion showed a more uniform particle size distribution, which was explained by its high emulsifying activity and stability (EAI: 49.5 m/g, ESI: 59.5 min). The interface rheology results showed that the alkaline pH-shifting treatment could promote the protein rearrangement and subsequently formed interface film with higher rate of protein penetration and rearrangement. The quantitative analysis of adsorbed proteins in the RPI-10 stabilized emulsion showed that glutelin-type isoforms as major proteins in RPI were increased at the oil-water interface for their balanced distribution of the hydrophilic and hydrophobic amino acid group. These quantitative and interfacial rheology analysis could improve deep understanding of the interfacial properties of pH-shifting treated RPI, and promote the development of application in grain protein stabilized emulsion.