Abstract: The aim of this study is to investigate gel-forming characteristics of white croaker protein itself. This study was carried out under the inhibition of the polymerization and degradation of myosin heavy chain (MHC) by ethylenediaminetetraacetic acid and leupeptin. The heat-induced gels were prepared by preheating at temperatures in the range of 30-80°C for 20 min or 2 h and then heating at 80°C for 20 min and were evaluated in terms of gel strength. In order to investigate the behavior of proteins, sodium dodecyl sulfate-polyacrylamide gel electrophoresis was carried out. Folin method was used to clarify the degradation of proteins by protease. Suwari occurred during preheating at 40 and 50°C and it contributed to gel-strengthening effect of the 2-step heating gels preheated at 50°C, indicating that non-covalent bonding reinforced the gel during setting and subsequent heating at 80°C even under the inhibition of the polymerization and degradation of MHC. The gel strength of 2-step heating gels was not affected by preheating temperature for 20 min, except for the gel preheated at 50°C under the inhibitory condition. Those gel strength values were similar to that of the gel heated directly at 80°C for 20 min. The maximum gel strength was obtained at 50°C. This suggests the gel-forming ability of white croaker protein itself. At temperature above 60°C, the gel strength decreased with preheating time, though the degradation of MHC was suppressed, indicating that non-proteolytic modori contributes to the weakening of gel of white croaker surimi.