ABSTRACT
Proteins, the most important functional components in muscle, confer many of the desirable physicochemical and sensory attributes of muscle foods. Muscle proteins comprise 15-22% of the total muscle weight and can be divided into three major groups on the basis of solubility characteristics: sarcoplasmic proteins, myofibrillar proteins, and stromal proteins. The functional behavior of myofibrillar proteins is manifested by their ability to produce three-dimensional, viscoelastic gel matrices via protein-protein interactions, to bind water, and to form cohesive and strong membranes on the surface of fat globules in emulsion systems or flexible films around the air/water interface. Proteins that are located inside the sarcolemma and are soluble in low salt concentrations are referred to as sarcoplasmic proteins. Sarcoplasmic proteins comprise about 30-35% of the total muscle proteins or about 5.5% of the weight of muscle in mature animals. Myosin is a large, fibrous protein with a molecular weight of about 500,000.
