Multifaceted functionality of l-arginine in modulating the emulsifying properties of pea protein isolate and the oxidation stability of its emulsions

Abstract

The effects of L-arginine (Arg) at different concentrations (0%, 0.05%, 0.1%, 0.2%, 0.5% and 1.0%) on the antioxidant activity, structure and emulsifying properties of pea protein isolate (PPI) were explored. The intrinsic mechanisms of the reactions at different concentrations were specifically examined. With an increase in Arg concentration, the scavenging activities of ABTS+˙ and ˙OH and the Fe²⁺ chelating activity of PPI increased significantly (P < 0.05). The addition of Arg (0%–0.2%) significantly modified the PPI structure, causing an increase in protein solubility (from 66.2% to 79.0%) and a decrease in protein particle size (from 682 nm to 361 nm) (P < 0.05). In addition, treatment with Arg (0%–0.2%) effectively improved the emulsifying activity of PPI (by 28%), decreased the droplet size and viscosity of the emulsion, and enhanced the physical and oxidation stabilities of the emulsion. The increase in interfacial protein content and the absolute value of ζ-potential, and the microscopy images also showed that 0%–0.2% Arg treatment helped in forming a uniform and stable microemulsion. In contrast, a high concentration (0.5%–1.0%) of Arg diminished its positive effect on the emulsifying properties of PPI. Therefore, treatment with an appropriate concentration of Arg can significantly improve the emulsifying activity of PPI and enhance the stability of the emulsions.