Differences in properties of myofibrillar proteins from bovine semitendinosus muscle after hydrostatic pressure or heat treatment

Hydrostatic pressure (HP) and heat treatments of myofibrillar proteins have both been shown to induce protein denaturation, but different gel formation properties result from these treatments. To characterise differences in the properties of proteins resulting from HP or heat treatment, Ca‐ and Mg‐ATPase activities (ATP, adenosine triphosphate) and protein solubility in 0.1 and 0.6 mol L^?1 KCl buffers (pH 7) were evaluated in this study. The inactivation rate of Ca‐ATPase of myofibrillar proteins (Mf) induced by HP was slower than that of Mg‐ATPase at each of the tested pressures. However, the inactivation rate of Ca‐ATPase induced by heating was faster than that of Mg‐ATPase at each of the tested temperatures. The level of soluble proteins in Mf suspension induced by HP in 0.1 mol L^?1 KCl buffer increased with increasing pressure up to 400 MPa and then decreased slightly at 500 MPa. However, the level of soluble proteins in Mf suspension induced by heat treatment in 0.1 mol L^?1 KCl buffer increased with increasing temperature up to 55°C. According to the results of sodium dodecyl sulfate polyacrylamide gel electrophoresis, the levels of soluble myosin heavy chain and actin in Mf suspension induced by HP in 0.6 mol L^?1 KCl buffer decreased simultaneously at pressures higher than 300 MPa. The level of soluble MHC in 0.6 mol L^?1 KCl buffer decreased gradually with increasing temperature, but there were no changes in the level of soluble actin in 0.6 mol L^?1 KCl buffer with increasing temperature up to 50°C. These results showed that the mechanism of HP‐induced protein denaturation was different from the mechanism underlying heat‐induced protein denaturation. Copyright © 2006 Society of Chemical Industry