This study investigates the effects of pulsed electric field (PEF) treatment on the structural and functional properties of quinoa protein isolate (QPI). The results show that PEF treatment significantly alters the secondary structure of QPI, converting random coils into β-sheets, which improves structural order and thermal stability. PEF treatment also reduces particle size, increases surface hydrophobicity, and enhances solubility, foaming, and emulsifying properties of QPI. The optimal PEF treatment conditions were found to be 7.5 kV/cm for 30 pulses. SEM analysis revealed that PEF treatment caused structural changes, including reduced particle size and altered microstructure. FTIR and UV spectroscopy confirmed changes in the secondary structure and tertiary structure of QPI, with PEF treatment increasing β-sheet content and hydrophobicity. SDS-PAGE analysis showed no significant changes in molecular size, indicating that PEF treatment did not alter the primary structure of QPI. The thermal stability of QPI was improved by PEF treatment, with higher denaturation temperatures and enthalpy values. Functional properties such as solubility, foaming capacity, and emulsifying activity were significantly enhanced by PEF treatment, with the best results observed at 7.5 kV/cm for 30 pulses. Overall, PEF treatment improved the structural and functional properties of QPI, making it a more promising protein source for food applications.This study investigates the effects of pulsed electric field (PEF) treatment on the structural and functional properties of quinoa protein isolate (QPI). The results show that PEF treatment significantly alters the secondary structure of QPI, converting random coils into β-sheets, which improves structural order and thermal stability. PEF treatment also reduces particle size, increases surface hydrophobicity, and enhances solubility, foaming, and emulsifying properties of QPI. The optimal PEF treatment conditions were found to be 7.5 kV/cm for 30 pulses. SEM analysis revealed that PEF treatment caused structural changes, including reduced particle size and altered microstructure. FTIR and UV spectroscopy confirmed changes in the secondary structure and tertiary structure of QPI, with PEF treatment increasing β-sheet content and hydrophobicity. SDS-PAGE analysis showed no significant changes in molecular size, indicating that PEF treatment did not alter the primary structure of QPI. The thermal stability of QPI was improved by PEF treatment, with higher denaturation temperatures and enthalpy values. Functional properties such as solubility, foaming capacity, and emulsifying activity were significantly enhanced by PEF treatment, with the best results observed at 7.5 kV/cm for 30 pulses. Overall, PEF treatment improved the structural and functional properties of QPI, making it a more promising protein source for food applications.