Bird muscles under hydrostatic high-pressure/temperature combinations

Abstract

Breast muscles from three different birds were subjected to hydrostatic high-pressure (400 MPa)/temperature (10–75°C) combinations, and the denaturation-induced effects on the pressurized proteins monitored by DSC. Comparisons with parallel results from heating-alone processes were established. Actin was the most labile moiety to pressurization and myosin together with sarcoplasmic proteins were next in observing pressure-induced denaturation at low temperatures. Some myosin derivatives (fragments or aggregates) and collagen remained native-like under pressure at any temperature.

As previously reported, pressure and temperature showed interdependent and antagonistic-like effects. Hydrostatic high-pressure caused severe proteins denaturation at non thermal denaturing temperatures. At thermally active conditions, pressure preserved proteins from subsequent thermal denaturation. This last effect was lower than in similar but destructured myosystems (batters) because of the absence of functional salts but presumably also by steric hindrance.