Abstract:Millet is an important source of high-quality proteins and the content of gliadin is particularly high.The effect of processing method on the structure and digestibility of gliadin has increasingly come to our attention.This study aims to explore the influence of heating（100℃，120℃，140℃，160℃，and 180℃ for 25 min）and glycosylation with D-xylose on the structure and digestibility of millet gliadin.The results showed that the glycosylated gliadin showcased the decrease in content of α-helix and random coil，surface hydrophobicity，intrinsic fluorescence intensity，free sulfhydryl content，and digestibility，and increase in β -sheet content and disulfide bond content with the rise of heating temperature.The gliadin which was only heated demonstrated the same variation pattern of the above indexes with the glycosylated gliadin except the surface hydrophobicity，and glycosylation had more significant effect on the protein.Pearson's correlation analysis suggested that β-sheet content and disulfide bond content of millet gliadin were highly correlated with protein digestibility.Therefore，heating and glycosylation can orderly increase structural elements of millet gliadin，make the protein structure more compact，and cause intermolecular aggregation，which will reduce the digestibility of the protein.The findings are expected to lay a theoretical basis for further exploring the influence of heating on the structure and nutrient digestion characteristics of millet protein.