Abstract
The dynamical properties of the pressure-induced gelation process of the muscle protein was investigated by observing the evolution of the turbidity spectra in the pressure-jump experiments. In the pressure-induced gelation process, time dependence of the slope of ln (τ d ) vs. ln λ (τ : turbidity, d : the thickness of the specimen and λ : wavelength) showed quite different behavior compared with the heat-induced one. Namely, as the time passed, the slope once decreased and then increased, suggesting that the depolymerization of F-actin takes place before the gelation process. Also, the surfaces of the pressure-treated products examined with a scanning electron microscope revealed the more smooth structure than that of the heat-induced gel.
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