The gelation properties of myofibrillar proteins are essential for the formation and stabilization of meat emulsions. Meat emulsions are produced by comminuting meat in the presence of lipid and water, resulting in an aqueous protein phase, wherein small lipid globules are dispersed. The lipid globules are stabilized by myofibrillar proteins, acting asmembrane proteins coating the globules, where myosin has been shown more effective than actin. The discontinuous lipid phase is immobilized to form a strong protein network generated by thermally induced protein–protein interactions between the proteins in the continuous phase and the membrane surface-active proteins. The immobilization by the dense protein network prevents coalescence of the lipid globules as well as water droplets, and ensures that the lipid and water is held finely dispersed in the continuous aqueous protein phase, resulting in a stable meat emulsion. Physical and chemical forces, including hydrophobic and ionic interactions, hydrogen bonds, van der Waal's interactions, and covalent bonds, such as disulfides, between the myofibrillar proteins in the continuous phase and myofibrillar proteins acting as membrane proteins, stabilize the lipid globules and are found to affect texture, moisture retention, and lipid stabilization in meat emulsions