Abstract
The heat-induced gelation of actomyosin (or natural actomyosin) treated with high pressure was investigated by dynamic rheological measurements. When actomyosin at 0.6 M HCl and pH 6.0 was subjected to a pressure of 150 MPa for 5 min, the dynamic rheological behavior during heat gelation showed a pattern similar to that of myosin. That is, the rheological transition in the 46-53 o C range induced by the presence of F-actin disappeared. The storage modulus (G') of pressurized actomyosin at 80 o C was almost double that observed in unpressurized actomyosin
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