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Myosin denaturation in pale, soft, and exudative (PSE) porcine muscle tissue as studied by differential scanning calorimetry
Author(s) -
Stabursvik Eva,
Fretheim Kristen,
Frøystein Terje
Publication year - 1984
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740350218
Subject(s) - denaturation (fissile materials) , myosin , differential scanning calorimetry , myofibril , chemistry , actin , biophysics , anatomy , biochemistry , biology , nuclear chemistry , physics , thermodynamics
Abstract Myofibrillar tissue from pale, soft, and exudative (PSE) pork was compared to tissue from normal pork by differential scanning calorimetry at pH 5.4. Thermograms of myofibrillar tissue from normal pork were characterised by three major peaks with temperature maxima at 58 and 66°C, associated with myosin denaturation, and at 78°C, associated with actin denaturation. In thermograms of PSE pork, the peak at 58°C was markedly reduced, and appeared as a shoulder. When the thermograms were divided into segments corresponding to the three major peaks, the area of the low temperature myosin segment was shown to be reduced by about 50% in PSE pork, as compared to normal pork. This indicates approximately 50% denaturation of the least thermostable parts of the myosin molecule. The more thermostable parts of the myosin molecule were largely unaffected, as was actin.