Abstract
The effects of different salt additions (1.0%, 1.5%, 2.0%, 2.5%, 3.0%, and 3.5%) on the gelling properties and protein phosphorylation of the mixed gels (MG) formed by silver carp (Hypophthalmichthys molitrix) surimi with 10% crabmeat were investigated. The MG's breaking force, deformation, gel strength, and water-holding capacity (WHC) increased as the salt concentration increased. The intrinsic fluorescence intensity of the samples initially decreased and then increased, reaching the lowest when the NaCl concentration was 2.5%. The result of SDS-polyacrylamide gel electrophoresis indicated that large aggregates were formed by protein-protein interaction in the MG containing 2.5% or 3.0% NaCl, decreasing the protein band intensity. It was also found that with the addition of NaCl, the phosphorus content initially increased and then decreased, reaching the maximum when the NaCl concentration was 2% or 2.5%, which was similar to the changing trend of actin band intensity reported in the results of Western blot. These results revealed that the amount of salt used had a significant effect on the degree of phosphorylation of the MG protein. The increase in phosphorylation was linked to improved gelling properties, which could lead to new ideas for manufacturing low-salt surimi products in the future.