Relationships between Binding Quality of Meat and Myofibrillar Proteins

Abstract

The viscosity change of myosin A concentrated solution with or without other components was measured as the incubation time elapsed at 30°C. The viscosity of myosin A solution increased, but that of F-actin solution did not. The shear stress at 0.04 sec⁻¹ was not increased to 1.0 dyne/cm² in the former, but in the latter was below 0.5 dyne/cm². The viscosity of myosin B solution increased slightly, but that of native tropomyosin-free myosin B solution decreased remarkably. In both the shear stress at 0.04 sec⁻¹ was greater than or equal to 15 dynes/cm². The speed of the viscosity increase in the presence of 3 mm pyrophosphate and 3 mm MgCl₂ was higher in concentrated solution of myosin B than in that of native tropomysin-free myosin B. The shear stress at 0.04 sec⁻¹ after 6 hr at 30°C was 11.5 and 8.2 dynes/cm², respectively. The effect of native tropomyosin and actin on the viscosity change was discussed.