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The role of conformational state of pea protein fractions on the oil/water dynamic adsorption, rheological interfacial properties and emulsifying properties

Recently, the utilization of pea protein is on the rise because of its low price and nutritional benefits. However, the application of pea proteins is still limited by its functional properties as compared to other plant proteins due to insufficient research, especially in structure-functionality relationship among individual pea protein fractions. Regarding the functional properties, emulsifying properties is one of the important functional properties of protein. It is well established that the emulsifying properties of protein is affected by protein composition, structural properties and environmental factors. As such, the aim of this study was to investigate the impact of environmental pHs (3, 7, 9) and different salt concentrations (20 mM, 200 mM) on protein structure, kinetic adsorption and rheological interfacial properties of pea protein fractions (globulin, legumin, vicilin and albumin) at the oil/water interface, and then to research its relationship with emulsifying properties. The results showed that the addition of NaCl had a greater impact when compared to pH for all tested pea protein fractions in a number of direction. For instance, the secondary structure of the protein was changed, the ability of the protein to increase the interfacial pressure (Ï€) was reduced. Consequently, the emulsifying capacity was also decreased. With regard to the fraction effect, legumin subunit had higher emulsifying stability when compared to vicilin. For example, the particle size of legumin stabilized emulsion increased slightly, but that of vicilin stabilized emulsion droplet increased dramatically (from 4.78 to 19.43 Î¼m) after 24 h storage at pH 3. This phenomenon might be attributed to the higher macromolecular interactions of vicilin at oil/water interface (e.g., the slopes of E- Ï€ plots were 2.18 legumin vs 3.19 vicilin). The research results could provide valuable information on molecular mechanism of emulsifying properties of pea protein fractions.