Gelation of myosin filaments under high hydrostatic pressure was investigated. At room temperature myosin filaments in 0.1 M KCl and 20 mM phosphate, pH 6.0, formed gels at 280 MPa and a protein concentration above 2 mg/ml or at 210 MPa and 3 mg/ml. However, no pressure-induced gelation was observed at 140 MPa. The gel strengths of pressure-induced gels were almost proportional to the protein concentration and they were comparable to those of heat-induced gels. The association of myosin filaments and the structural disturbance seemed to coincide with the formation of the gel. The microstructure of the pressure-induced myosin gel consisted of a fine network and was similar to that of heat-induced myosin filament gels at low ionic strength. Myosin light chains 1 and 3 were easily dissociated from the pressure-induced gels.
Yamamoto, Katsuhiro; Miura, Takeo; and Yasui, Tsutomu
"Gelatin of Myosin Filament Under High Hydrostatic Pressure,"
4, Article 7.
Available at: http://digitalcommons.usu.edu/foodmicrostructure/vol9/iss4/7