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 m2/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.