Corn gluten meal is a by-product of starch production that is readily available. Corn protein isolates have limited applications due to their hydrophobic nature, low solubility and limited functionality as emulsifiers. In this study, a mild acidic treatment of corn gluten meal was performed in order to achieve deamidation of asparagine and glutamine residues and modify the interfacial behavior of this byproduct. A 0.1 N HCl treatment for 6 h at 70 °C rendered a deamidation degree of 20.4%, which increased the emulsification activity index of corn gluten meal from 6.8 to 16.8 m²/g protein, with a remarkable increase in emulsion stability from 0 to 90.6% oil retention. Proteins participating in the emulsion were separated by SDS-PAGE and the main polypeptides were identified as alpha and beta-zeins. After deamidation, protein dissociation and unfolding due to the obtained negative charges resulted in enhanced functionality.