Bird
muscles under hydrostatic high-pressure/temperature combinations |
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Authors: | F Fernández-Martín |
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Institution: | (1) Department of Engineering, Institute of Refrigeration (CSIC), Ciudad Universitaria, Madrid, Spain, 28040 |
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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. |
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Keywords: | chicken denaturation-preservation effects DSC myofibrillar proteins ostrich pressure-temperature treatments turkey |
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