This study investigated the cross-linking of myosin with pH₁₂-shifted legumin (11S_pH) or vicilin (7S_pH), and the gel properties of composite gels, with or without transglutaminase, in 0.3 M NaCl. The free sulfhydryl content of 7S_pH/11S_pH increased significantly (P < 0.05). The covalent cross-linking degree between 7S_pH/11S_pH and myosin was enhanced, with the vicilin of approximately 45 kDa showing more pronounced cross-linking. SDS–PAGE analysis of myosin subfragments revealed that S1 and light meromyosin were the primary cross-linking regions for 11S_pH, reducing the Ca²⁺-ATPase activity of the myosin head, while S2 was an alternative cross-linking region for 7S_pH. The cross-linking of 7S_pH/11S_pH enhanced the thermal aggregation of S1. The cross-linking degree of tails followed this order: myosin > myosin+7S_pH > myosin+11S_pH. Thus, the use of 7S_pH/11S_pH and transglutaminase offers a new approach to improving texture in low-salt meat products.