Relationship between the water molecules in fish-meat gel and the gel structure

To elucidate the structure of the network of the water retention mechanism of fish-meat gel, the microscopic relationship between the water content and viscoelasticity was investigated, and the specific surface area (S) where the water molecules are adsorbed was also measured. The gel structures of fish-meat, actomyosin (AM), and myosin (M) were investigated. In the fish-meat gel, as the water content increased, the number of network chains (nu) decreased and the molecular weight between the cross-linking points (M (e)) increased. At 10 % salinity and approximately 79 % moisture, nu decreased to a minimum and M (e) began to increase remarkably. In addition, when the moisture increased to 78 %, S increased about 1.5 times and the elasticity decreased significantly, indicating that this level of water content is the limit for sufficiently forming a gel structure in fish-meat gel. In the AM and M gels, M (e) and S were similar to those observed in the fish-meat gels. When the moisture content increased, they also increased, regardless of the salt concentration. This result suggests that the size of the network was enlarged or that the network chains were cleaved.