The purpose of the present study was to investigate the effects of cryoprotectants (4 % sucrose + 4 % sorbitol) on functional and rheological changes, including thermal stability, dynamic rheological and emulsifying properties, gel texture profile, gel whiteness, gel water-binding capacity, and gel microstructure, in the myofibrillar proteins (MP) of common carp (Cyprinus carpio) surimi subjected to multiple freeze-thaw cycles (FT, 0, 1, 3 and 5 times). Increased numbers of FT cycles were accompanied by reduced thermal transition temperature (T (max)), reduced enthalpy of denaturation (Delta H) (P < 0.05), and enhanced susceptibility to thermal aggregation. The observation of the gel microstructure indicated that the FT processes produced empty spaces and changed the aggregate gel structure into a coarser-stranded network. The addition of cryoprotectants significantly prevented the reduction of MP thermal stability (P < 0.05). The protective effect on protein functionality was demonstrated by the cryoprotectant's efficacy in maintaining the three-dimensional gel network by small-strain oscillatory rheological testing and increasing the emulsifying capacity and emulsion stability of the MP. The FT process caused a decrease (P < 0.05) in whiteness, water-binding capacity, and texture (hardness, springiness, and gumminess) of the MP gels, which were reduced by the addition of cryoprotectants. Overall, the FT-induced loss of the abovementioned functional and rheological properties was significantly reduced by the presence of cryoprotectants.