Abstract: The present study aimed to investigate the impact of heat treatment on the interaction between gliadin and rutin by intrinsic fluorescence spectroscopy, Fourier transform infrared spectroscopy, surface hydrophobicity measurement and scanning electron microscopy. For this purpose, gliadin-rutin complex was heat treated at 25, 60, 80 or 100 ℃ for 30 min. Gliadin was regarded as the control. Further, soybean oil emulsion stabilized with the treated complex was prepared and evaluated for their rheological properties. After the formation of the emulsion, the changes in potential, viscosity and microstructure were observed and frequency scanning and amplitude scanning were carried out. The results indicated that appropriate temperature treatment had significant effects on the surface hydrophobicity and microstructure of the protein, improved the viscosity of the emulsion, and enhanced the stability of the emulsion. The potential of the emulsion stabilized with gliadin-rutin complex treated at 80 ℃ was the highest among all temperatures tested, up to + 16.58 mV, indicating the highest emulsion stability. This provides a theoretical basis for the application of gliadin in dairy foods.

Key words: gliadin; rutin; rheological properties; emulsion