Role of pH in gel formation of washed chicken muscle at low ionic strength

This work was designed to test the hypothesis that it is not solubilization of the myofibrillar proteins per se that is required to form good gels at low salt concentrations, but the protein-containing structures must be diso rganized. Gels were made from washed minced chicken breast muscle at 0.15, 0.88, and 2.5% sodium chloride. The gels made with varying salt concentrati ons were evaluated either at pH 6.0-6.5 or pH 7.0-7.4. Strain values, an in dicator of protein quality, were high only at neutral pH in the gels contai ning 0.15 or 0.88% salt. At 2.5% salt, strain values of gels made at acid p H were superior to those at the low salt concentrations at acid pH, but inf erior to gels with 2.5% salt at neutral pH. Poor gels were obtained at 0.15 % salt and low pH whether or not there was an intermittent adjustment to ne utral pH. A neutral salt wash markedly increased the water content of the m ince, suggesting that solubility-inhibiting proteins were removed. Good qua lity gels were obtained in the absence of any detectable solubilization of myosin and only minimal solubilization of actin.