Herring surimi during low temperature setting, physicochemical and textural properties

Herring surimi was held at 10 degrees C for 0 to 24 hr, then heated at 90 degrees C for 30 min. Rigidity, shear stress and shear strain at failure increased with holding time at 10 degrees C, and the values of shear strain were greater than or equal to 2.0 when setting time was >3 hr. Electrophoresis revealed three types of protein-protein interactions involved in the formation of myosin polymers during setting at 10 degrees C and/or subsequent heating at 90 degrees C. The interactions included covalent, nondisulfide interactions; disulfide bonds and noncovalent interactions. The contributions of each type of protein-protein interaction to the formation of myosin polymers varied with setting time. Variations in the types of interactions were related to physical/chemical properties.