Comparative impacts of physical and chemical modifications on pea protein concentrate: Effects on physicochemical properties

Pea proteins are promising plant-based ingredients; however, their limited solubility restricts broader application. While pea protein isolates are widely studied, the modification of pea protein concentrate remains underexplored. This study compared four modification methods, two physical modifications (dry heating and ultrasonication), and two chemical modifications (pH shifting and Maillard conjugation with guar gum) to improve the solubility of pea protein concentrate. Optimal conditions were: dry heating (80 °C, 30 min), ultrasonication (70% amplitude, 5 min), pH shifting (pH 10, 3 h), and Maillard reaction (60 °C, 1 h). All treatments altered solubility, surface charge, hydrophobicity, particle size, and protein structure. Ultrasonication and pH shifting achieved the highest solubility improvements (96.4% and 92.62%, respectively, from an initial 73.1%). Maillard conjugation increased hydrophobicity but had a limited impact on solubility, with only a 6% increase, while dry heating showed the least change. Overall, all modifications increased the surface hydrophobicity of the proteins, while the proportions of α-helix and β-turn structures increased in all treatments except the conjugated protein. These findings indicate that each method affects pea protein concentrate differently, highlighting the importance of selecting techniques based on the intended application.