Nuclear magnetic resonance instruments (NMR), Fourier transform infrared spectrometer (FITR), differential scanning calorimetry (DSC), dynamic rheometers (DHR) and scanning electron microscopy (SEM) were used to study the effect of polyγ-glutamicacid (γ-PGA) addition on the stability of gluten protein during frozen storage. Gluten protein was measured on days 0, 7, 21, 35 and 49, respectively. The thermal hysteresis activity of γ-PGA was measured by DSC. The results showed that γ-PGA had good antifreeze activity. The obtained results showed that supplementation with 1% γ-PGA lowered the conversion of immobilized water to free water in gluten during frozen storage. γ-PGA inhibited the decrease of αhelix and the increase of random coil during frozen storage, and the addition of γ-PGA significantly increased the α-helix content. The results of DSC and TGA showed that the addition of γ-PGA improved the thermodynamic stability of gluten protein. The denaturation temperature of gluten protein increased by 4℃, and the increase in weight loss caused by frozen storage was also smller than that of the control group. With the extension of frozen storage time, the decrease of G′ and G″ of gluten protein added with γ-PGA was lower than that of control group. The electron microscope results showed that the gluten network structure with γ-PGA added was more uniform, smaller in pore size and better in continuity after 49d of frozen storage. The above results indicate that γ-PGA can effectively inhibit the growth and recrystallization of ice crystals, weaken the destruction of gluten network by frozen storage, and improve the frozen storage stability of gluten.