Abstract: In order to explore the structure and function characteristics of wheat globulin in noodle processing, the effect of wheat globulin addition on the quality of cooked noodles was investigated under alkali (Na₂CO₃) and salt (NaCl) conditions. And the interaction between globulin and gluten protein was further explored. The texture and tensile properties of cooked noodles were measured with texture profile analysis. The results showed that the hardness and springiness of cooked noodles with the addition of globulin were significantly improved under alkaline condition. While, the boost from salt was not obvious. Further analysis of the molecular structure of the noodle protein was performed. When globulin was added alone, the number of disulfide bonds increased. In addition, the increase of disulfide bonds was greater under alkali condition, indicating that the protein aggregation with disulfide bonds during cooking occurred, and the synergistic effect of globulin and alkali accelerated the disulfide bonds cross-linking in the gluten-globulin complex, while the effect of salt was not obvious. In addition, Fourier infrared spectrometry was conducted to analyze the protein secondary structure. The results showed that the β-sheets and α-helixes reduced and the β-turns increased when only globulin was added; under alkali induction, the β-sheets were significantly increased, meanwhile, the α-helixes and β-turns were significantly decreased. Under salt induction, the β-sheets increased and the β-turns decreased after globulin addition, while the changes were slighter than those under alkali induction, in addition, the change of random coils and α-helixes were not obvious. The results showed that the hydrogen bonding interaction between the proteins was significantly enhanced under alkali induction. Furthermore, the fluorescence spectroscopy was conducted to explore the protein surface hydrophobicity. The results showed that the protein surface hydrophobicity decreased when globulin was added alone; under alkali induction, the decrease of the protein surface hydrophobicity was significantly smaller after globulin addition. However, under salt induction, the protein surface hydrophobicity was increased. These results indicated that the hydrophobic interaction between globulin and gluten protein was further weakened under alkali and salt induction. In conclusion, the alkali induced obvious enhancement of hydrogen and disulfide bond interactions between globulin and gluten protein, which promoted the aggregation of the protein network and then significantly improved the noodle processing quality.