Considerable research has been done to better understand the basis for gel formation by myofibrillar proteins (MPs) in effort to manufacture acceptable processed meats with lower cost and more desirable nutritional characteristics. Results from research available indicate that there is no substitute for the myofibrillar protein myosin in gel formation by proteins from a wide variety of animal and fish species. This report consolidates information on determinants of protein gel formation, examining types of muscles and fibers, the species influence, and interactions of the MPs actin and myosin with each other and with fat, gelatin, starch, hydrocolloids, some protein soy, whey, and nonprotein additives such as phosphates and acidifiers, and the influences of pH, ionic strength, rates of heating, and its absence, protein oxidation, as well as the use of transglutaminase and high hydrostatic pressure. It is of interest that myosin alone will form acceptable gels. Gel formation by MPs is optimized at pH 6, an ionic strength of 0.6 M, and at 60 to 70 °C. The observations that collagen-derived gelatin can reduce the rubbery texture of low-fat products and that solubilization of MPs is not always essential for gel formation, and the observation that good gels can be formed in the absence of salt, are exciting developments that should be considered as pressure mounts to continue to reduce fat and salt in the diet.

https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1541-4337.2010.00137.x

Factors Influencing Gel Formation by Myofibrillar Proteins in Muscle Foods

Investigation on fish surimi gel as promising food material for 3D printing

Li-hong Qin

Papers

Role of secondary structures in the gelation of porcine myosin at different pH values.

Effect of pH on the gel properties and secondary structure of fish myosin