This work explores enhancing gliadin's functional performance through Maillard reaction-based conjugation with starch hydrolysates and glucose. Four novel conjugates were prepared: gliadin-starch hydrolysates (UGli-Cor1, UGli-Cor2, UGli-Cor3) and gliadin-glucose (UGli-Cor4). The formation of these conjugates was confirmed via grafting efficiency, SDS-PAGE, and FT-IR analysis. Conjugation efficiency varied with the molecular weight of starch hydrolysates, following the order: UGli-Cor4 (24.9 %) >
UGli-Cor3 (19.3 %) >
UGli-Cor2 (15.51 %) >
UGli-Cor1 (9.34 %). Structural analysis showed that the covalent attachment of starch hydrolysates altered gliadin's spatial conformation, enhancing its solubility and emulsifying properties. Notably, the conjugation site influenced the quantity of conjugated starch hydrolysates and the emulsifying performance. Conjugates attached to the N-terminal domain of gliadin exhibited superior emulsifying abilities compared to those attached to the C-terminal domain. Moreover, conjugates with higher grafting degrees showed enhanced emulsifying performance, assuming the conjugation site remained constant. This work provides a theoretical foundation for improving the functionality of gliadin, which would widely expand its applications in the food sector and beyond.