“…The low solubility at pH 4 is due to the fact that this pH is close to the pH of the isoelectric point (pI) of the 11S quinoa globulin (around 5) since there are no repulsive charges, which leads to protein association and precipitation (Kaspchak et al, ). In contrast, the solubility of QPI, QPI‐HD, and QPI‐FL at pH 10 was significantly higher ( p < .05) compared to the values found at pH 4 and 7, possibly due to higher pH at the isoelectric point favoring a change in the structure of the protein that produces a greater exposure of the hydrophilic proteins, increasing the surface polarity and its interaction with water (Elsohaimy et al, ; Kaspchak et al, ; Mäkinen et al, ). Furthermore, it has been reported that at pH values higher than isoelectric point value, there are negative charges on the protein, causing more interaction with the solvent and increase of solubility (Ruiz, Xiao, Van Boekel, Minor, & Stieger, ).…”