Abstract: In order to explore the effect of antifreeze protein (AFP) on the water-holding capacity and texture of frozen scallop (Patinopecten yessoensis) adductor muscle, muscle samples were vacuum-impregnated in aqueous solutions containing each of the three antifreeze agents, 0.2 g/100 mL AFP, 3.0 g/100 mL sodium pyrophosphate and 3.0 g/100 mL trehalose. The yield, centrifugal loss, texture, color, moisture distribution and mobility, ice crystal morphology and microstructural structure of these samples were detected. The results showed that the hardness, cohesiveness and brightness of proton density images of the AFP group were in agreement with those of the fresh sample, and were significantly higher than those of the sodium pyrophosphate and trehalose groups. Compared with the other groups, the yield, springiness and shear force of the AFP group were significantly increased, and T21 relaxation time was significantly shortened (P < 0.05). As observed by optical microscopy and scanning electron microscopy (SEM), the ice crystals in the AFP group were small and spherical, and the muscle fiber structure was clear and complete. The average cross-sectional area of ice crystals was 65.06% lower than that in the blank group, treated with NaCl. This study confirmed that AFP can adsorb onto the surface of ice crystals to inhibit their growth and modify their shape. It is more effective than sodium pyrophosphate and trehalose in regulating the water-holding capacity and texture of frozen scallop muscle and thus can be considered as an effective means to control the quality of frozen products.

Key words: Patinopecten yessoensis adductor muscle; antifreeze protein; vacuum impregnation; water-holding capacity; texture