The ginkgo seed protein isolate (GSPI) solution and pullulan (PULL) solution were mixed to obtain a final GSPI concentration at 120 g/L, which contains 25, 50, and 100 g/L PULL, respectively. Following lyophilization of the mixed solutions, the GSPI-PULL conjugates were incubated at 70°C and 63% relative humidity for 1-7 d. The effect of conjugation on the heat-induced gel texture softening was investigated by characterizing the physicochemical properties of the GSPI-PULL conjugations, along with the physiochemical properties and microstructure of the GSPI-PULL gels. It was demonstrated that PULL is capable of conjugating with GSPI, and their grafting degree depends on both PULL concentration and reaction time. A heating effect promoted the unfolding of the protein structure, and conjugation reactions brought hydrophilic groups into the protein. The unfolding of the protein structure was facilitated by a heating effect, and hydrophilic groups were introduced to the protein through conjugation reactions. Heating and conjugation both attenuate GSPI gelation, and were of composite effects, resulted in GSPI gels changing from a "standing solid" to a "semisolid/sol", achieved the heat-induced protein gels with tunable textural properties.