한국축산식품학회지 (Food Science of Animal Resources)

  • 제31권5호
  • /
  • Pages.676-683
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  • 2011
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  • 2636-0772(pISSN)
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  • 2636-0780(eISSN)
한국축산식품학회 (Korean Society for Food Science of Animal Resources)
권호 표지
DOI QR코드

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Comparison of Physicochemical Characteristics of Hot-boned Chicken Breast and Leg Muscles during Storage at 20℃

  • Yu, Long-Hao (College of Food Science, Heilongjiang Bayi Agricultural University) ;
  • Lee, Eui-Soo (Genesis BBQ) ;
  • Chen, Hong-Sheng (College of Food Science, Heilongjiang Bayi Agricultural University) ;
  • Jeong, Jong-Youn (Muscle Biology and Meat Science, University of Wisconsin) ;
  • Choi, Yun-Sang (Food and Biological Resources Examination Division, Korean Intellectual Property Office) ;
  • Lim, Dong-Gyun (Korea Livestock Products HACCP Accreditation Service) ;
  • Kim, Cheon-Jei (Department of Food Science and Biotechnology of Animal Resources, Konkuk University)
  • 투고 : 2011.05.20
  • 심사 : 2011.09.19
  • 발행 : 2011.10.31
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초록

The aim of this study was to compare the physicochemical changes of hot-boned chicken breast and leg muscles. Chicken breast and leg muscles from 56 broilers were excised within a 15 min post-mortem (PM) and stored at $20^{\circ}C$. Physicochemical traits were determined at 0.5, 6, 12, and 24 h PM. The ultimate pH of leg muscle was higher than that of breast muscle (p<0.05). The content of glycogen in the breast muscle was relatively higher than that in the leg muscle until 6 h PM (p<0.05). R-values showing rigor mortis of breast and leg muscles were completed after or before 6 h PM. Breast muscle had less cooking loss than leg muscle (p<0.05). Drip loss did not significantly differ between breast and leg muscles with the exception of that at 6 h PM. The sarcomere length of leg muscle was relatively longer than that of breast muscle (p<0.05). The MFI of leg muscle was significantly lower than that of breast muscle (p<0.05). The shear force of leg muscle was lower than that of breast muscle at 6 and 12 h PM (p<0.05); however, that of both muscles did not significantly differ at 24 h PM.

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참고문헌

  1. Beecher, G. R., Cassens, R. G., Hoekstra, W. G., and Briskey, E. J. (1965) Red and white fiber content and associated postmortem properties of seven porcine muscles. J. Food Sci. 30, 969-976. https://doi.org/10.1111/j.1365-2621.1965.tb01872.x
  2. Botka-Petrak, K., Vidacek, S., Petrak, T., and Medicì, H. (2005) Influence of combined, continuous chilling on physical and chemical properties of white and red chicken muscles. Veterinarski Arhiv. 75, 415-422.
  3. Calkins, C. R., Dutson, T. R., Smith, G. C., and Carpenter, Z. L. (1982) Concentrations of creatine phosphate, adenine nucleotides and their derivatives in electrically stimulated and nonstimulated beef muscle. J. Food Sci. 47, 1350-1353. https://doi.org/10.1111/j.1365-2621.1982.tb07683.x
  4. Cason, J. A. C., Lyon, E. and Dickens, J. A. (2002) Tenderization of hot-boned broiler breast meat by clamping during chilling. Poultry Sci. 81, 121-125. https://doi.org/10.1093/ps/81.1.121
  5. Chang, Y.S. and Chou, R.G. (2010) Postmortem degradation of desmin and calpain in breast and leg and thigh muscles from Taiwan black-feathered country chickens. J. Sci. Food Agric. 90, 2664-2668. https://doi.org/10.1002/jsfa.4137
  6. Choe, J. H., Nam, K. C., Jung, S. M., Kim, B. N., Yun, H. J., and Jo, C. R. (2010) Differences in the quality characteristics between commercial Korean native chickens and broilers. Korean J. Food Sci. Ani. Resour. 30, 13-19. https://doi.org/10.5851/kosfa.2010.30.1.13
  7. Cooper, T. G. (1977) Biuret protein determination. In "The tools of biochemistry". John Wiley & Sons, New York. p. 51.
  8. Daum-Thunberg, D. L., Foegeding, E. A., and Ball, H. R. Jr. (1992) Rheological and water-holding properties of comminuted turkey breast and thigh: effects of initial pH. J. Food Sci. 57, 333-337. https://doi.org/10.1111/j.1365-2621.1992.tb05488.x
  9. de Fremery, D. and Pool, M. F. (1960) Biochemistry of chicken muscle as related to rigor mortis and tenderization. Food Res. 25, 73-87. https://doi.org/10.1111/j.1365-2621.1960.tb17938.x
  10. Dreiling, C. E., Brown, D. E., Casale, L., and Kelly, L. (1987) Muscle glycogen: comparison of iodine binding and enzyme digestion assays and application to meat samples. Meat Sci. 20, 167-177. https://doi.org/10.1016/0309-1740(87)90009-X
  11. Farouk, M. M. and Lovatt, S. J. (2000) Initial chilling rate of pre-rigor beef muscles as an indicator of colour of thawed meat. Meat Sci. 56, 139-144. https://doi.org/10.1016/S0309-1740(00)00031-0
  12. Fernandez, X., Lefaucheur, L., and Candek, M. (1995) Comparative study of two classifications of muscle fibres: consequences for the photometric determination of glycogen according to fibre type in red and white muscle of the pig. Meat Sci. 41, 225-235. https://doi.org/10.1016/0309-1740(94)00059-G
  13. Geesink, G. H., Koolmees, P. A., van Laack, H. L. J. M., and Smulders, E. J. M. (1995) Determinants of tenderisation in beef longissimus dorsi and triceps brachii muscles. Meat Sci. 41, 7-17. https://doi.org/10.1016/0309-1740(94)00066-G
  14. Hamm, D. (1983) Techniques for reducing toughness in hotstripped broiler meat. Poultry Sci. 62, 1430.
  15. Hopkins, D. L. and Thompson, J. M. (2002) Factors contributing to proteolysis and disruption of myofibrillar proteins and the impact on tenderisation in beef and sheep meat. Aust. J. Agric. Res. 53, 149-166. https://doi.org/10.1071/AR01079
  16. Jeacocke, R. E. (1977) Continuous measurements of the pH of the beef muscle in intact beef carcasses. J. Food Technol. 12, 375-386.
  17. Kandeepan, G., Anjaneyulu, A. S. R., Kondaiah, N., Mendiratta, S. K., and Lakshmanan, V. (2009) Effect of age and gender on the processing characteristics of buffalo meat. Meat Sci. 83, 10-14. https://doi.org/10.1016/j.meatsci.2009.03.003
  18. Khan, A. W. (1971) Effects of temperature during post-mortem glycolysis and dephosphorylation of high energy phosphates on poultry meat tenderness. J. Food Sci. 36, 120-121. https://doi.org/10.1111/j.1365-2621.1971.tb02050.x
  19. Kim, O. H., Park, C. I., and Park, Y. S. (1996) Effect of chitosan additive feeding on the tenderness of broiler meat. Korean J. Food Sci. Ani. Resour. 16, 62-66.
  20. Koh, K. C., Binder, T. D., McMillan, K. W., and Kim, M. B. (1993) The relationship between ATP and R-values in postmortem bovine longissimus dorsi muscle. Meat Sci. 33, 253-263. https://doi.org/10.1016/0309-1740(93)90063-N
  21. Lametsch, R., Knudsen, J. C., Ertbjerg, P., Oksbjerg, N., and Therkildsen, M. (2007) Novel method for the determination of myofibril fragmentation post-mortem. Meat Sci. 75, 719-724. https://doi.org/10.1016/j.meatsci.2006.10.002
  22. Lawrie, R. A. (1991) Meat science. 5th ed, Pergamon Press, New York.
  23. Lee, Y. B., Hargus, G. L., Webb, J. E., Rickansrud, D. A., and Hagberg, E. C. (1979) Effect of electrical stimulation on post-mortem biochemical changes and tenderness in broiler breast muscle. J. Food Sci. 44, 1121-1122. https://doi.org/10.1111/j.1365-2621.1979.tb03461.x
  24. Lesiak, M. T., Olson, D. G., Lesiak, C. A., and Ahn, D. U. (1996) Effects of post-mortem temperature and time on the water-holding capacity of hot-boned turkey breast and thigh muscle. Meat Sci. 43, 51-60. https://doi.org/10.1016/0309-1740(95)00062-3
  25. Lesiow, T. and Xiong, Y. L. (2003) Chicken muscle homogenate gelation properties: effect of pH and muscle fiber type Meat Sci. 64, 399-403. https://doi.org/10.1016/S0309-1740(02)00206-1
  26. Liu, A., Nishimura, T., and Takahashi, K. (1996) Relationship between structural properties of intramuscular connective tissue and toughness of various chicken skeletal muscles. Meat Sci. 43, 43-49. https://doi.org/10.1016/0309-1740(95)00065-8
  27. Liu, G. and Xiong, Y. L. (1996) Contribution of lipid and protein oxidation to rheological differences between chicken white and red muscle myofibrillar proteins. J. Agric. Food Chem. 44, 779-784. https://doi.org/10.1021/jf9506242
  28. Lyon, B. G. and Hamm, D. (1986) Effects of mechanical tenderization with sodium chloride and polyphosphates on sensory attributes and shear values of hot-stripped broiler breast meat. Poultry Sci. 65, 1072-1707.
  29. Lyon, C. E., Hamm, D., and Thomson, J. E. (1985) pH and tenderness of broiler breast meat deboned various times after chilling. Poultry Sci. 64, 307-310. https://doi.org/10.3382/ps.0640307
  30. McKee, S. R. and Sams, A. R. (1998) Rigor mortis development at elevated temperatures induces pale exudative turkey meat characteristics. Poultry Sci. 77, 169-174. https://doi.org/10.1093/ps/77.1.169
  31. Northcutt, J. K., Foegeding, E. A., and Edens, F. W. (1994) Water-holding properties of thermally preconditioned chicken breast and leg meat. Poultry Sci. 73, 308-316. https://doi.org/10.3382/ps.0730308
  32. Nowsad, A. A. K. M., Kanoh, S., Niwa, E. (2000) Thermal gelation characteristics of breast and thigh muscles of spent hen and broiler and their surimi. Meat Sci. 54, 169-175. https://doi.org/10.1016/S0309-1740(99)00091-1
  33. Olson, D. G., Parrish, F. C. Jr., and Stromer, M. H. (1976) Myofibril fragmentation and shear resistance of three bovine muscles during post-mortem storage. J. Food Sci. 41, 1036-1041. https://doi.org/10.1111/j.1365-2621.1976.tb14384.x
  34. Papa, C. M. and Fletcher, D. L. (1988) Pectoralis muscle shortening and rigor development at different locations within the broiler breast. Poultry Sci. 67, 635-640. https://doi.org/10.3382/ps.0670635
  35. Prado, C. S. and de Felício, P. E. (2010) Effects of chilling rate and spray-chilling on weight loss and tenderness in beef strip loin steaks. Meat Sci. 86, 430-435. https://doi.org/10.1016/j.meatsci.2010.05.029
  36. Purchas Roger, W., Triumf Ellen, C., and Egelandsdal, B. (2010) Quality characteristics and composition of the longissimus muscle in the short-loin from male and female farmed red deer in New Zealand. Meat Sci. 86, 505-510. https://doi.org/10.1016/j.meatsci.2010.05.043
  37. SAS (1996) User's Guide: Statistics. Version 6th ed, SAS Institute, Inc., Cary, NC. USA.
  38. Seabra, L. M., Zapata, J. F., Fuentes, M. F., Aguiar, C. M., Freitas, E. R., and Rodrigues, M. C. (2001) Effect of deboning time, muscle tensioning, and calcium chloride marination on texture characteristics of chicken breast meat. Poultry Sci. 80, 109-112. https://doi.org/10.1093/ps/80.1.109
  39. Stewart, M. K. and Fletcher, D. L. (1984) The influence of hot boning broiler breast muscle and pH decline and toughening. Poultry Sci. 63, 1935-1939. https://doi.org/10.3382/ps.0631935
  40. Toohey E S, Hopkins D L, Stanley D F, and Nielsen S G. (2008) The impact of new generation pre-dressing mediumvoltage electrical stimulation on tenderness and colour stability in lamb meat. Meat Sci. 79, 683-691. https://doi.org/10.1016/j.meatsci.2007.10.036
  41. Vega-Warner, V., Merkel, R. A., and Smith, D. M. (1999) Composition, solubility and gel properties of salt soluble proteins from two bovine muscle types. Meat Sci. 51, 197-203. https://doi.org/10.1016/S0309-1740(98)00101-6
  42. Voyle, C. A. (1971) Sarcomere length and meat quality. Proceed. 17th Eur. Meeting Meat Res. Workers, Bristol, England, pp. 95-97.
  43. Wattanachant, S., Benjakul, S., and Ledward, D. A. (2004) Composition, color, and texture of Thai indigenous and broiler chicken muscles. Poultry Sci. 83, 123-128. https://doi.org/10.1093/ps/83.1.123
  44. Wyche, R. C. and Goodwin, T. L. (1974) Hot-cutting of broilers and its influence on tenderness and yield. Poultry Sci. 53, 1668-1675. https://doi.org/10.3382/ps.0531668
  45. Young, L. L. and Lyon, C. E. (1997) Effect of calcium marination on biochemical and textural properties of peri-rigor chicken breast meat. Poultry Sci. 76, 197-201. https://doi.org/10.1093/ps/76.1.197
  46. Yu, L. H., Lee, E. S., Jeong, J. Y., Paik, H. D., Choi, J. H., and Kim, C. J. (2005) Effects of thawing temperature on the physicochemical properties of pre-rigor frozen chicken breast and leg muscles. Meat Sci. 71, 375-382. https://doi.org/10.1016/j.meatsci.2005.04.020

피인용 문헌

  1. Sensory Quality Evaluation of Superheated Steam-Treated Chicken Leg and Breast Meats with a Combination of Marination and Hot Smoking vol.10, pp.8, 2011, https://doi.org/10.3390/foods10081924