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Relationship between Thermal Properties of Muscle Proteins and Pork Quality 원문보기

Asian-Australasian journal of animal sciences, v.18 no.3, 2005년, pp.427 - 432  

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)

Abstract AI-Helper 아이콘AI-Helper

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 ...

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제안 방법

  • longissimus dorsi between the 5th and the 11th pork rib was obtained within half hour after slaughtering from the slaughterhouse. Samples were package with polyethylene film and then chilled/stored at -2℃ or 25℃ (ambient temperature) for 0, 12, 24, 36, 48 or 96 h for analyses.
  • , 1983), and ion strength (Kijowski and Mast, 1988; Barbut and Findlay, 1991). The purpose of this study was performed as model study using four animals to investigate changes of DSC thermograms associated to freshness parameters including pH value, bacterial counts, ATP-related compounds, volatile basic nitrogen (VBN) levels and K-values. SDS-PAGE patterns were also evaluated.

대상 데이터

  • The animals used in this study were 100 kg of body weight LYD pigs (n=4). Two kg m.

데이터처리

  • Data were analyzed using a statistics software package (SAS, 1995). The GLM system was used to calculate regress correlation. When significant (p<0.
  • When significant (p<0.05) overall differences were found, differences between individual means were then assessed by Duncan’s multiple range tests.
  • The GLM system was used to calculate regress correlation. When significant (p<0.05) overall differences were found, differences between individual means were then assessed by Duncan’s multiple range tests.

이론/모형

  • The enthalpy of muscle proteins denaturation was also collected. Electrophoretic behavior of muscle proteins was carried out by the method of Laemmli (1970). One gram of M.
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참고문헌 (30)

  1. AOAC. 1984. Official methods of Analysis, 14th ed., Association of Official American Chemists. Washington. DC. USA. 

  2. 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. 

  3. 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. 

  4. 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. 

  5. 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. 

  6. 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. 

  7. 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. 

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

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

  10. 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. 

  11. 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. 

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

  13. 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. 

  14. 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. 

  15. 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. 

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

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

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

  19. 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. 

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

  21. 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. 

  22. 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. 

  23. 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. 

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

  25. 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. 

  26. 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. 

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

  28. 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. 

  29. 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. 

  30. 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. 

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