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The aim of this study was to evaluate the effect of HHP and rigor state on palm ruff (Seriolella violacea) muscle proteins. HHP treatments were performed at 450-550 MPa for 3 and 4 min at 15°C. Protein secondary structure was evaluated by using Fourier transform infrared spectroscopy, and the thermal behavior was evaluated by using differential scanning calorimetry. The results showed that HHP treatments reduced a-helix and increased b-sheet in fish protein structures. Throughout the 35-d storage period, secondary structures in HHP samples changed depending on pressure intensity, holding time, and rigor state. The thermograms of palm ruff muscles showed four endothermic transitions in prerigor state and three in postrigor state. The HHP treatment affected thermal stability of myosin protein, which is reflected in the change of denaturation temperature (T d ) and a decrease in denaturation enthalpy (DH d ) with respect to the native protein; actin was denatured by the pressure treatments. In conclusion, rigor state and HHP affected protein structure of fish proteins.

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