The sample solution was subjected to different conditions (25， 60， 80 and 100 ℃， for 30 min). Multiple spectroscopic techniques were used to characterize the interaction between gliadin and rutin and the emulsifying properties of the complex caused by temperature. The particle size， potential， thermal stability， emulsification activity and emulsification stability of the composite were determined to observe the changes in the functional properties of the composite under heat induction conditions. The results shown that proper temperature treatment (80 ℃) made a remarkable difference in the particle size [increased to (330.34±2.70)nm] and potential [increased to (19.30±0.67) mV] of the G-R solution， which can promote the unfolding of protein structure and improve the emulsification properties of the complex. The emulsification activity and emulsification stability of the complex after treatment at 80 ℃ were the highest， which were (105.71±0.86) m2/g and (85.94±2.92) min， respectively. This research provided new ideas for the functional modification and structural modification of gliadin.