Abstract:Quinoa seeds are rich in proteins, which can be used as an ingredient in food protein sources. White, red, and black quinoa seeds are commonly found, and their protein content and functional properties may differ. In this study, the proteins were isolated and extracted from white, red, and black quinoa varieties, and the physicochemical and functional properties of white quinoa protein isolates (WQPI), red quinoa protein isolates (RQPI), and black quinoa protein isolates (BQPI) were studied under different pH conditions (2.0–10.0) and NaCl concentrations (0–0.6 mol/L). In all three protein isolates, acidic and basic subunits are cross-linked via disulfide bonds, resulting in 11S globulins, along with a small amount of 7S globulins, although their relative contents differ. Protein particle size and surface charge were highly dependent on pH, and their surface hydrophobicity significantly decreased as pH increased. Overall, protein solubility, emulsifying activity, and foaming capacity were significantly enhanced at pH values away from the isoelectric point, while foam stability decreased. The gelling and interfacial properties of WQPI and RQPI were better than those of BQPI under neutral conditions. Concentration-dependent effects of NaCl on protein solubility, emulsification, and foaming were observed. Moreover, WQPI and RQPI gelled markedly better than BQPI.