Physicochemical properties and heat-induced gelling of cardiac myosin in model system.

Somephysicochemical and functional properties of cardiac myosin were studied in a model system, with particular reference to its binding ability in re-structured meat.Wefound that myosin solubility was strongly influenced by the pH, ionic strength, and temperature of the system and by the interaction of pH and ionic strength.For instance, myosin remained completely in solution in monomeric form at ionic strengths ^0.2m KC1, if the pH of system was maintained at 7.0.High ionic strength was required to keep myosin in monomericform at low pH.With low ionic strength and pH, myosin molecules tend to form aggregated filaments.