In order to explore the impact of TGase from different species of freshwater fish on gel properties， the effect of silver carp transglutaminase （STG） or black carp transglutaminase （BTG） on the solubility， protein aggregation， rheological properties， puncture properties， and microscopic morphology of myosin after low-temperature gelation were evaluated. Results showed that the addition of STG/BTG promoted formation of more ε-（γ-Glu）-Lys covalent bonds in myosin heavy chain （MHC） of silver carp or black carp compared with the group without enzyme addition， resulting in more aggregation of MHC. The turbidity and average particle size of myosin， the elastic modulus（G'）， breaking force， and breaking distance of myosin gel increased significantly， and the protein network structure was enhanced. In terms of enhancing the gel properties of the same myosin， the catalytic cross-linking effect of BTG was stronger than that of STG， while the activity of BTG （12.67 U/mg） was lower than that of STG （14.34 U/mg）， and the myosin gel properties of black carp were always higher than those of silver carp regardless of TGase addition. In conclusion， the essential reason for the differences in gel properties of surimi from different freshwater fish species was the source of myosin rather than the differences in TGase activity.