Microstructure and Biochemistry of Avian Muscle and its Relevance to Meat Processing Industries

Abstract

This review is an attempt to summarize information concerning the gross and microscopic anatomy of avian muscle. In addition, specific proteins found in muscle tissue such as the troponins, tropomyosin, alpha- and beta-actinin, desmin, vimentin, myomesin, and creatine kinase are described. The role of protein synthesis and degradation, leading to net protein accumulation in growing animals, is addressed. It is thought that learning to decrease the rate of protein degradation would have immense economic significance. Satellite cells are mentioned as some of these cells fuse with muscle cells to become true muscle nuclei. Understanding the mechanism by which the nuclei of satellite cells differentiate into muscle nuclei could lead to a practical means of increasing protein synthesis within muscle tissue. Finally, postmortem biochemistry is discussed to show how the pH of muscle tissue interacts with environmental temperature to affect the final tenderness of the product.

Effect of Chilling Method and Deboning Time on Broiler Breast Fillet Quality

“…Temperature of the breast muscle during postmortem aging has been demonstrated to affect fillet quality [8,24,25,26,27,28]. Previous studies have indicated that elevated temperatures or slower chilling rates may accelerate postmortem glycolysis and ultimate meat texture and functional properties [29,30,31,32,33,34,35,36,37].…”

Influence of Selected Oven and Endpoint Temperatures upon the Ultrastructure of Turkey Meat

“…The TEM (Fig. 1B,D,F,H) show the classical structures reported by Dutson and Carter (1985). Fiber coverings appear partially torn off in the SEM (Fig.…”

Comparative Microstructure of Red Meat, Poultry and Fish Muscle

“…1974). Toughness also relates to the relaxation state of the muscle during rigor and its resolution (Dutson et al 1976). Seafood muscle passes through rigor about as rapidly as pork and chicken and the changes associated with rigor are similar.…”