Abstract: Abstract: Abalone (Haliotis discus hannai) is an important commercial seafood species. Pleopod muscle is the edible part of abalone, which is rich in protein and mainly composed of myofibril protein and collagen. The change in conformation and aggregation of protein during heating would affect the quality of the product. Chemical interactions including hydrogen bonds, disulfide bonds, non-disulfide bonds, ionic bonds, and hydrophobicity have shown great effect on textural properties of muscle protein. This study used the method of grading extraction solution, scanning electronic microscopy (SEM), and Fourier transform infrared (FTIR) to investigate the law of changes in chemical interactions and textural properties of the abalone (Haliotis discus hannai Ino) pleopod muscle protein. The results indicate that as the temperature increases (60℃, 80℃, 100℃), the changes of chemical interaction in the center and the edge or transition part of the abalone muscle protein were similar. During heating, the content of ionic and hydrogen bonds declined; the content of hydrophobic bonds first increased and then decreased whereas disulfide and non-disulfide bonds increased but the increasing amount differed due to the different composition of protein. The center part is characterized by high amounts of myofibrilllar protein while the edge or transition part contains more collagen. The textural property shows the following changes: during low temperature (60℃), the harness, resilience, springiness, cohesiveness, and chewiness of the abalone muscle were low. As the temperature increased, the parameters changed significantly. However, the harness and chewiness of the edge or transition part of the abalone muscle protein decreased slightly when temperature increased to 100℃. The results of SEM suggest that fresh abalone muscle exhibited a porous net structure composed of a vast amount of layers. However, as heating temperature increased (60℃, 80℃, 100℃), a porous closed-knit structure with a tiny hole was formed both in the center and the edge or transition part of the abalone muscle. FTIR analysis indicates that the secondary structure of protein changed significantly; the N-H bond bended, C-N bond stretched and vibrated, α-helix showed non-regular curved structure, hydrophobicity of myofibrillar protein increased, and disulfide bonds were formed. In addition, there were close correlations between chemical interactions and textural characteristics, which indicate that ionic, hydrogen, and hydrophobic bonds played important roles in the soft gel during the low temperature (60℃) period. However disulfide and non-disulfide bonds were the main chemical interaction for the formation and maintenance of gel with excellent harness, springiness, and cohesiveness at the high temperature period (80℃, 100℃). Our results not only expose the change of the secondary structure of the abalone muscle protein during the heating-gel forming process but also provide information on the relationship between chemical interactions and textural properties. The study provides useful information on the mechanism of protein changes in the pleopod muscle of abalone during heating and on the processing techniques of the abalone muscle.