IONIC, PH, AND TEMPERATURE EFFECTS ON THE BINDING ABILITY OF MYOSIN

The peak force required to separate pieces of meat at a binding junction was measured with the Instron Universal Testing Machine. These measurements were used to study the effects of salt, phosphate, pH, cooking temperature and. protein concentration on the ability of crude myosin to bind meat pieces. Results showed salt and phosphate to linearly increase the ability of myosin to bind meat pieces primarily by solubilizing the protein. Temperature and the level of protein had increasing effects on binding ability in the range 45‐80°C and 0‐8%, respectively. Scanning electron micrographs of the ultrastructure of gels formed by myosin showed a three dimensional network of overlapping fibers in the presence of salt and phosphate and a sponge‐like network in their absence. Since the ultrastructure of the gel formed by myosin heavy chains was comparable to that of myosin, it was concluded that the heavy chain core of the myosin molecule plays an important role in the heat‐induced gelation of myosin. The relationship between the formation of a three dimensional network of fibers by the heavy chains of myosin and the mechanism of binding meat pieces was discussed. Copyright © 1979, Wiley Blackwell. All rights reserved