Abstract
This study examined some physicochemical properties of actomyosin isolated from pre-rigor chicken breast muscle (Pectoralis major) to gain insight on its interaction with 0.2–1.0M sodium bicarbonate (NaHCO3) either with or without 3% sodium chloride (NaCl). NaHCO3 has been a frequent quality raiser with respect to water holding capacity of meat, which is adversely affected at low pH. This study document a remarkable inactivation of ATPases and the weakening of actin-myosin interaction with increasing molarity of NaHCO3, irrespective of the presence or absence of NaCl. Similarly, there was a concomitant increase in turbidity of soluble fraction, increase in total protein solubility and reactive SH groups. The observations on protein solubility/insolubility are supported by SDS-PAGE profiles. Therefore, the conformational changes induced by NaHCO3 are concentration dependent and appear different from those during thermal transitions. The findings suggest that low concentration of NaHCO3 may be more suitable component of marinades, since it affects the main myofibrillar contractile complex less adversely.
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