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Relationship between Thermal Properties of Muscle Proteins and Pork Quality

Kuo, Hsiu-Lan    (Department of Food Nutrient, Chung-Hwa College of Medical Technology   ); Chen, Ming-Tsao    (Department of Food Nutrient, Chung-Hwa College of Medical Technology   ); Liu, Deng-Cheng    (Department of Animal Science, National Chung-Hsing University   ); Lin, Lieh-Chin    (Department of Animal Science, National Chung-Hsing University  );
  • 초록

    The purpose of this study was performed as model study using four animals to investigate the correction between the changes in Differential Scanning Calorimetry thermogram of muscle proteins during storage and meat freshness. M. longissimus dorsi of pork was obtained immediately after slaughter and chilled/stored at either $-2^{\circ}C$ or $25^{\circ}C$ for up to 96 h for analyses. DSC thermograms were determined and compared with pH values, ATP-related compounds, K-values, volatile basic nitrogen (VBN) levels, bacterial counts and electrophoretic behavior. Changes in pH, bacterial counts, VBN and K-values were associated with increased storage temperature and time. The levels of pH values, bacterial counts, VBN and K-values of pork samples stored at $25^{\circ}C$ were higher than those of the pork samples stored at $-2^{\circ}C$ . ATP concentration decreased faster in samples stored at $25^{\circ}C$ . Only IMP increased in samples stored at $-2^{\circ}C$ , whereas the concentration of hypoxanthine and inosine increased in samples stored at $25^{\circ}C$ . One exothermic peak and two endothermic peaks appeared on the thermograms of pork stored at either temperature. Lower transition temperature of myosin, sarcoplasmic protein and actin peaks were observed. The freshness parameters of K-value, VBN and hypoxanthine showed highly negative correlations (-0.742- -0.9980) to the changes in transition temperature. Therefore, the shift temperature on DSC thermogram can be used as an indicator of the freshness parameters of meat.


  • 주제어

    Association .   Productive Traits .   Polymorphism .   Lipoprotein Lipase Gene .   Pigs.  

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