DOI QR코드

DOI QR Code

Physico-chemical Properties and Changes of Sarcoplasmic Protein Bands of Chicken Meat Cuts with or without Salt during Cooking Temperatures

식염첨가 유무에 따른 계육의 부위별 가열온도에 따른 이화학적 성상과 근장 단백질 밴드의 변화

  • Kim, Soo-Hee (Dept. of Animal Science and Institute of Agricultural Science and Technology, Chonnam National University) ;
  • Chin, Koo-Bok (Dept. of Animal Science and Institute of Agricultural Science and Technology, Chonnam National University)
  • 김수희 (전남대학교 동물자원학부 및 농업과학기술연구소) ;
  • 진구복 (전남대학교 동물자원학부 및 농업과학기술연구소)
  • Published : 2007.04.30

Abstract

This study was performed to measure the pH, proximate composition, physicochemical properties, changes of protein bands, Hunter color values and endpoint cooking temperature of chicken leg and breast muscles during cooking from 64 to 74℃ with 2℃ increments. Chicken leg had higher pH, moisture and fat contents (%) and lower protein solubility(P<0.05) than chicken breast. Although the cooking losses(CLs, %) of chicken muscles increased with increased cooking temperature, the addition of 2% salt did not affect CL. The redness values of chicken leg without 2% salt were higher than chicken breast, however, the addition of 2% salt reduced the differences of the redness. Protein solubility decreased with increased cooking temperatures and were not affected by the addition of salt, and no further changes were observed higher than 68℃. Protein bands having the molecular weights of 66 and 54kDa were disappeared in the chicken leg at the cooking temperatures of 66~70℃, whereas 66, 54 and 34kDa in the chicken breast. These protein bands could be used potential indicators to determine the endpoint cooking temperature in chicken muscles.

Keywords

Chicken leg and breast muscles;Protein bands;Endpoint cooking temperature

References

  1. Kim, Y. J. and Park, C. I. 2001. Effects of additions of activated carbon on productivity and physico-chemical characteristics in broilers. Kor. J. Food Sci. Ani. Resour. 21(1):24-31
  2. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685 https://doi.org/10.1038/227680a0
  3. Lee, J. E, Jung, I. C, Kim. M. S. and Moon, Y. H. 1994. Postmortem changes in pH, VBN, total plate counts and k-value of chicken meat. Kor. J. Food Sci. Resour. 14:240-244
  4. Lowry, O. H., Rosebrogh, J. M., Farr, A. L. and Randdall, R. J. 1951. Protein measurement with the folin phenol reagent. J. Biol. Chem. 193:265- 275
  5. Maltin, C. A., Warkup, C. C., Matthews, K. R., Porter, A. D. and Delday, M. I. 1997. Pig musle fibre characteristics as a source of variation in eating quality. Meat Sci. 47:237-248 https://doi.org/10.1016/S0309-1740(97)00055-7
  6. Park, C. I. 2002. Effect of dietary mugwort on the physico-chemical properties of chicken meat. Kor. J. Food Sci. Ani. Resour. 22(3):212-217
  7. Ruusunen, M., Vainionpaa, J., Lyly, M., Lahteen- maki, L., Niemisto, M., Ahvenainen, R. and Puolanne, E. 2005. Reducing the sodium content in meat products; The effect of the formulation in low-sodium ground meat patties. Meat Sci. 69:53- 60 https://doi.org/10.1016/j.meatsci.2004.06.005
  8. USDA-FSIS. 1994. Requirements for the production of cooked beef, roast beef and cooked corn beef. Code of Federal Regulations, Title 9, Ch. 3, Part 318.17. Office of the Federal Register, National Archives and Records Administration. Washington, D
  9. Xiong, Y. L. and Brekke, C. J. 1989. Change in protein solubility and gelation properties of chicken myofibers during storage. J. Food Sci. 54(5): 1141-1146 https://doi.org/10.1111/j.1365-2621.1989.tb05941.x
  10. 농림부. 2006. 주요국별 1인당 주요 육류소비량. 농림부 주요 통계. pp. 352
  11. AOAC. 1995. Official method of analysis. 16th edition. Association Official Analytical Chemists International. Washington DC
  12. Huffman, D. L., Cross, H. R., Campbell, K. J. and Cordray, J. C. 1981. Effect of salt and tripolyphosphate on acceptability of flaked and formed hamburger patties. J. Food Sci. 46:34-36 https://doi.org/10.1111/j.1365-2621.1981.tb14524.x
  13. Hwangbo, S. and Chung, K. Y. 1997. Purification and antibody production of chicken-specific muscle protein (50 kDa). Kor. J. Food Sci. Ani. Resour. 17(3):257-264
  14. Hwang C. S., Hong J. M. and Lee, K. H. 1975. Effects of cooking treatment on the composition of chicken meat( I ). Korean J. Anim. Sci. 17(2): 184-186
  15. Kang, S. M., Chin, K. B., Cho, S. H. and Lee, J. M. 2004. Physico-chemical properties and utiliza- tion of sarcoplasmic proteins for the determination of end-point cooking temperatures of ground pork hams contain salt and fat. Kor. J. Anim. Sci. and Technol. 46(1):83-90 https://doi.org/10.5187/JAST.2004.46.1.083
  16. Smith, D. M., Desrocher, A. M., Booren, C. H., Wang, C. H., Agouzied, M. M., Pestka, J. J. and Veeramuthu, G. J. 1996. Cooking temperature of turkey ham affects lactate dehydrogenase, serum albumin and immunoglobulin G as determined by ELISA. J. Food Sci. 61:209-212, 234 https://doi.org/10.1111/j.1365-2621.1996.tb14761.x