Gelatin of Myosin Filament Under High Hydrostatic Pressure

Authors

Katsuhiro Yamamoto, Rakuno Gakuen University
Takeo Miura, Rakuno Gakuen University
Tsutomu Yasui, Rakuno Gakuen University

Creative Commons License

This work is licensed under a Creative Commons Attribution 4.0 License.

Abstract

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.

Recommended Citation

Yamamoto, Katsuhiro; Miura, Takeo; and Yasui, Tsutomu (1990) "Gelatin of Myosin Filament Under High Hydrostatic Pressure," Food Structure: Vol. 9: No. 4, Article 7.
Available at: https://digitalcommons.usu.edu/foodmicrostructure/vol9/iss4/7