The changes of water-holding capacity， hardness， elasticity， soluble protein content， microscopic morphology and structure of soy protein isolate-dextran conjugate gels crosslinked by transglutaminase (TG) at different mass concentration(30，40，50，60 mg/mL) during freeze-thaw cycling (FTC) were explored. The Maillard reaction between soy protein isolate and dextran was confirmed by the results of SDS-PAGE electrophoresis. At the same time，soy protein isolate-dextran conjugates (SPI-D) were generated. With the Maillard reaction process proceeded， the grafting degree of SPI-D increased firstly and then decreased， finally reached the maximum of 12.54% at a mass concentration of 50 mg/mL. Surface hydrophobicity and fluorescence spectroscopy proved that the structure of the protein unfolded， flexibility and disorder enhanced， which was beneficial to the freeze-thaw stability. Compared with the control， the water-holding capacity of SPI-D， SPI and dextran mixture(SPI+D) and SPI gel decreased by 32.46%， 42.81% and 44.98%， the hardness increased by 124.66%， 271.51% and 343.38%， and the elasticity increased by 4.38%， 9.58% and 11.76%， the soluble protein content decreased by 2.05%， 3.61% and 7.17%， respectively， after 5 FTCs. Among these experimental groups，SPI-D gel showed the smallest change in all indicators and the best freeze-thaw stability， the microstructure of the gel was characterized by the scanning electron microscopy images， compared with SPI + D gel and SPI gel， SPI-D gel had smaller pores and more uniform organization. The above findings suggested that Maillard reaction was an effective technical means to enhance the freeze-thaw stability of soy protein isolate gel by enzyme method.