Abstract
Recent advances in muscle biology concerning the discoveries of a large variety of proteins have been described in this review. The existence of polymorphism in several muscle proteins is now well established. Various isoforms of myosin not only account for the difference in physiological functions and biochemical activity of different fiber types or muscles, but also seem to differ in functional properties in food systems. The functionality of various muscle proteins, especially myosin and actin in the gelation process in modal systems which simulate structured meat products, is discussed at length. Besides, the role of different subunits and subfragments of myosin molecule in the gelation mechanism, and the various factors affecting heat-induced gelation of actomyosin in modal systems are also highlighted. Finally, the areas which need further investigation in this discipline have been suggested.
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