Gel Color and Texture of Surimi-like Pork from Muscles at Different Rigor States Post-mortem

  • Kang, Geun-Ho (Poultry Research Division, National Livestock Research Institute, Rural Development Administration) ;
  • Yang, Han-Sul (Division of Applied Life Science and Technology, Graduate School, Gyeongsang National University) ;
  • Jeong, Jin-Yeon (Division of Applied Life Science and Technology, Graduate School, Gyeongsang National University) ;
  • Moon, Sang-Hoon (Division of Applied Life Science and Technology, Graduate School, Gyeongsang National University) ;
  • Hur, Sun-Jin (Division of Applied Life Science and Technology, Graduate School, Gyeongsang National University) ;
  • Park, Gu-Boo (Division of Applied Life Science and Technology, Graduate School, Gyeongsang National University) ;
  • Joo, Seon-Tea (Division of Applied Life Science and Technology, Graduate School, Gyeongsang National University)
  • Received : 2006.06.09
  • Accepted : 2006.12.06
  • Published : 2007.07.01


Gels were made from surimi-like pork (SLP) made from muscles obtained at 1, 24 and 72 h post-mortem. The SLP from pre-rigor muscle had higher pH and moisture percentage compared to in- or post-rigor muscles. Also, SLP from pre-rigor muscle showed higher concentration of water-soluble protein that was washed out during the process. Gel from post-rigor muscle exhibited higher a* and b* value, and also resulted in higher Chroma and lower hue values. The dark color of gel from post-rigor muscle was related to higher concentration of sarcoplasmic protein in SLP and denser structure in the gel matrix. SDS-PAGE showed higher intensity of the phosphorylase in the sarcoplasmic protein fraction from pre-rigor muscle. Gel from post-rigor muscle showed higher hardness and sensory firmness, and the greater firmness was related to higher concentration of protein in SLP, and a compact network with smaller pockets in the gel matrix.


Supported by : MOCIE


  1. Toyoda, K., I. Kimura, T. Fujita, S. F. Noguchi and C. M. Lee. 1992. The Surimi Manufacturing Process. In: Surimi technology (pp. 79-112). New York: Marcel Dekker Inc.
  2. SAS. 2001. The SAS program for window. Statistical Analysis System Institute, Cary, NC, USA.
  3. Park, J. W., T. C. Lanier and D. H. Pilkington. 1993. Cryostabilization of functional properties of pre-rigor and post-rigor beef by dextrose polymer and/or phosphate. J. Food Sci. 58:467-472.
  4. Park, S., M. S. Brewer, J. Novakofski, P. J. Bechtel and F. K. McKeith. 1996. Process and characteristics for a surimi-like material made from beef or pork. J. Food Sci. 61:422-427.
  5. Nowsad, A. A. K. M., S. Kanoh and E. Niwa. 2000. Thermal gelation characteristics of breast and thigh muscles of spent hen and broiler and their surimi. Meat Sci. 54:169-175.
  6. Offer, G. and J. Trinick. 1983. On the mechanism of water holding in meat: The welling and shrinking of myofibrils. Meat Sci. 8:245-281.
  7. Lee, S. K. and B. J. Min. 2004b. Effect of setting temperatures and time on the gelation properties (suwari and modori phenomena) of surimi from mechanically deboned chicken meat. Asian-Aust. J. Anim. Sci. 17:1758-1763.
  8. Lesiow, T. and Y. L. Xiong. 2003. Chicken muscle homogenate gelation properties: effect of pH and muscle fiber type. Meat Sci. 64:399-403.
  9. MacDougall, D. B. 1986. The chemistry of color and appearance. Food Chem. 21:283-289.
  10. An, H., M. Y. Peters and T. A. Seymour. 1996. Roles of endogenous enzymes in surimi gelation. Trends Food Sci. Technol. 7:321-327.
  11. Laemmli, U. K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227:680-685.
  12. Kang, G. H., C. Y. Han, S. T. Joo, B. C. Kim and G. B. Park. 2006. Effect of addition levels of sodium chloride on gel properties of surimi-like pork. Kor. J. Food Sci. Anim. Resour. 26:20-27.
  13. Katayama, K., K. B. Chin, S. Yoshihara and M. Muguruma. 2006. Microbial transglutaminase improves the property of meat protein and sausage texture manufacture with low-quality pork loin. Asian-Aust. J. Anim. Sci. 19:102-108.
  14. Joo, S. T., R. G. Kauffman, B. C. Kim and C. J. Kim. 1995. The relationship between colour and water-holding capacity in postrigor porcine longissimus muscle. J. Muscle Foods 6:211-226.
  15. Joo, S. T., R. G. Kauffman, B. C. Kim and G. B. Park. 1999. The relationship of sarcoplasmic and Myofibrillar protein solubility to colour and water-holding capacity in porcine longissimus muscle. Meat Sci. 52:291-297.
  16. Gornall, A. G., C. J. Bardawill and M. M. David. 1949. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177:751-766.
  17. Francis, F. J. and F. M. Clydesdale. 1975. The measurement of meat color. In: Food Colorimetry: Theory and Application, The AVI Publishing Company, Inc., Westport, CT. pp. 73-111.
  18. Hamm, R. 1981. Post-mortem changes in muscle affecting the quality of comminuted meat products. Ch. 4. In Developments in Meat Scinece-2, (Ed. R. Lawrie), Applied Science Publishers, Englewood, NJ. p. 93.
  19. Carroll, R. J. and C. M. Lee. 1981. Meat emulsions: Fine structure relationships and stability. Scanning Electron Microsc. 3:447-452.
  20. Folch, J., M. Lees and G. H. S. Stanley. 1957. A simple method for the isolation and purification of total lipids from animal tissues. J. Biol. Chem. 226:497-509.
  21. AOAC. 1990. Official Methods of Analysis. 15th edn. Association of Official Analytical Chemists, Arlington, Virginia, USA.
  22. Bourne, M. C. 1968. Texture profiling of ripening pears. J. Food. Sci. 33:223-226.
  23. Xiong, Y. L. and C. J. Brekke. 1990. Thermal transitions of salt-soluble proteins from pre- and postrigor chicken muscles. J. Food Sci. 55:1540-1543.
  24. Wang, B. and Y. L. Xiong. 1999. Characterization of the proteases involved in gel weakening of beef heart surimi. J. Agric. Food. Chem. 47:887-892.
  25. Wismer-Pederson, J. 1959. Quality of pork in relation to rate of pH changes post mortem. Food Res. 24:711-727.
  26. Lan, Y. H., J. Novakofski, T. R. Carr and F. K. McKeith. 1993. Assay and storage conditions affect yield of salt-soluble protein from muscle. J. Food Sci. 58:963-967.
  27. Lee, S. K. and B. J. Min. 2004a. Surimi quality from mechanically deboned chicken meat as affected by washing cycle, salt concentration, heation temperature and rate. Asian-Aust. J. Anim. Sci. 17:131-136.
  28. Antonomanolaki, R. E., K. P. Vareltzis, S. A. Georgakis and E. Kaldrymidou. 1999. Thermal gelation properties of surimi-like material made from sheep meat. Meat Sci. 52:429-435.
  29. Mansfield, B. 2003. Fish, factory trawlers, and imitation crab: the nature of quality in the seafood industry. J. Rural. Stud. 19:9-21.

Cited by

  2. Physicochemical changes of myosin and gelling properties of washed tilapia mince as influenced by oxidative stress and microbial transglutaminase pp.0975-8402, 2014,
  3. Quality of shrimp analogue product as affected by addition of modified potato starch vol.52, pp.7, 2015,
  4. ) and chicken mixture gels as affected by setting temperatures vol.21, pp.1, 2018,