Advanced SearchSearch Tips
Relationship between Thermal Properties of Muscle Proteins and Pork Quality
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
 Title & Authors
Relationship between Thermal Properties of Muscle Proteins and Pork Quality
Kuo, Hsiu-Lan; Chen, Ming-Tsao; Liu, Deng-Cheng; Lin, Lieh-Chin;
  PDF(new window)
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 or 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 were higher than those of the pork samples stored at . ATP concentration decreased faster in samples stored at . Only IMP increased in samples stored at , whereas the concentration of hypoxanthine and inosine increased in samples stored at . 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.
Association;Productive Traits;Polymorphism;Lipoprotein Lipase Gene;Pigs;
 Cited by
AOAC. 1984. Official methods of Analysis, 14th ed., Association of Official American Chemists. Washington. DC. USA.

Barbut, S. and C. J. Findlay. 1991. Influence of sodium, potassium and magnesium chloride on thermal properties of beef muscles. J. Food Sci. 56:180-182.

Boyle, J. L., R. C. Lindsay and D. A. Stuiber. 1991. Adenosine nucleotide degradation in modified atmosphere chill-stored fresh fish. J. Food Sci. 56:1267-1270.

Cannon, J. E., J. B. Morgan, J. Heavner, F. K. McKeith, G. C. Smith and D. L. Meeker. 1995. Pork quality audit: A review of the factors influencing pork quality. J. Muscle foods. 6:369-402.

Chen, M. T. and S. L. Guo. 1992a. Studies on the microbial flora of Chinese-style sausage. 2. Action of selected organisms isolated from Chinese-style sausage on porcine muscle proteins. Fleischwirt. 72:1126-1128.

Chen, M. T., C. P. Lee and D. C. Liu. 1992b. Studies on 2, 3- Diphosphoglycerate, pyruvate kinase and mitochondrial ATPase activities in PSS pig. Proceeding of 38th International Cong. Meat Sci. Technol. 3:345-346.

Chen, M. T., C. P. Lee and D. C. Liu. 1992. DSC Studies on thermal properties of muscle proteins in normal and PSE pork. Proceedings of 38th International Cong. Meat Sci. Technol. 3:347-350. France.

Ehira, S. 1976. A biochemical study on the freshness of fish. Bull. Tokai. Reg. Fish Res. Labor. 88:1-132.

Food and Drug Administration. 1975. FDA Bacteriological Analytical Manual for Food. 4th ed., FDA, Washington, DC. USA.

Goodno, C. C. and C. A. Swenson. 1975. Thermal transitions of myosin and its helical fragments. II. Solvent-induced variations in conformational stability. Biochem. 14:873-878.

Hamm, R. 1981. Postmortem changes in muscle affecting the quality of comminuted meat products. In 'Developments in Meat Sci. 2.' (Ed. R. Lawrie) Appl. Sci. Pub., Inc., London.

Hofmann, K. 1988. pH a quality criterion for meat. Fleischwirt. 68:67-70.

Hwang, I. H. and J. M. Thompson. 2002. A technique to quantify the extent postmortem degradation of meat ultrastructure. Asian-Aust. J. Anim. Sci. 15:111-116.

Jensen, K. N. and B. M. Jorgensen. 2003. Effect of storage conditions on differential scanning calorimetry profiles from thawed cod muscle. Lebensm-Wiss. U. Technol. 36:807-812.

Judge, M. D., E. D. Aberle, J. C. Forrest, H. B. Hedrick and R. A. Merkel. 1989. Principles of meat science. 2nd edition Kendall. pp. 85-133. Hunt pub. Co.

Kijowski, J. M. and M. G. Mast. 1988. Thermal properties of proteins in chicken broiler tissues. J. Food Sci. 53:363-366.

Kimura, I. O., S. M. Sugimoto and T. O. Fujita. 1987. Measurement of fish flesh freshness by DSC. Netsu Sokutei. 14:37-38. Japan.

Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 277:680-685.

Okuma, H. and E. Watanabe. 2002. Flow system for fish freshness determination based on double multi-enzyme reactor electrodes. Biosensor and Bioelectronics 17:367-372.

Park, J. W. and T. C. Lanier. 1988. Calorimetric changes during development of rigor mortis. J. Food Sci. 53:1312-1314, 1372.

Ryder, J. M. 1985. Determination of ATP and its breakdown products in fish muscle by high-performance liquid chromatography. J. Agric. Food Chem. 33:678-680.

Saito, T. K. Ara and M. Matsuyoshi. 1959. A new method for estimating the freshness of fish. Bul. Japan. Soc. Sci. Fish 24:249-250.

Samejima, K., M. Ishioroshi and T. Yasui. 1983. Scanning calorimetric studies on the thermal denaturation of myosin and its subfragments. Agric. Biol. Chem. 47:2373-2379.

SAS. 1995. SAS system for window 95 (Release 6.111). SAS Inst. Inc., Cary, USA.

Stabursvik, E. and H. Martens. 1980. Thermal denaturation of proteins in post-rigor muscle tissue as studies by differential scanning calorimetry. J. Sci. Food Agric. 31:1034-1042.

Stabursvik, E., K. Fretheim and T. Frostein. 1984. Myosin denaturation in pale, soft and exudative (PSE) porcine muscle tissue as studies by differential scanning calorimetry. J. Sci. Food Agric. 35:240-244.

Wagner, J. R. and M. C. Anon. 1985. Denaturation kinetics of myofibrillar proteins in bovine muscle. J. Food Sci. 50:1547-1550.

Watanable, A., H. Sato, E. Tsuneishi, M. Matsumoto and Y. Takimoto. 1992. Effect of slaughter methods on the postmortem changes of pH and ATP-related compounds of beef muscles. Jpn. Anim. Sci. Technol. 63:935-941.

Wright, D. J., I. B. Leach and P. Wilding. 1977. DSCC studies of muscle and its constituent proteins. J. Sci. Food Agric. 28:577-564.

Xiang, Y. L. and C. J. Brekke. 1990. Thermal transitions of salt soluble proteins from pre- and post-rigor chicken muscles. J. Food Sci. 55:1540-1543.