Thermal Gelation of Stretched and Cold‐Shortened Bovine Sternomandibularis Muscle and Myofibrils

Abstract

Muscle gels (10% protein) and myofibril gels (8% protein) were prepared at pH 6.0 with 2% NaCl and a heating rate of 0.7'C/min. No difference in gel strength occurred between stretched and cold-shortened muscles, but cooking loss was lower for stretched muscle. Stretched muscle sarcomeres were longer than those of cold-shortened muscle. The myofibril fraction from stretched muscle had higher gel strength, viscosity index, elasticity, and lower cooking loss than that from cold-shortened muscle. These results suggest that the contractile state of the muscle affects protein binding and water binding of the myofibrillar fraction.