Food Science and Biotechnology

Korean Society of Food Science and Technology (한국식품과학회)
권호 표지

Effects of Thawing Temperature on the Physicochemical and Sensory Properties of Frozen Pre-Rigor Beef Muscle

  • Lee, Eui-Soo (Department of Applied Microbiology and Food Science, University of Saskatchewan) ;
  • Jeon, Jong-Youn (Department of Food Science and Biotechnology of Animal Resources, Konkuk University) ;
  • Yu, Long-Hao (National Livestock Research Institute, Rural Development Administration) ;
  • Choi, Ji-Hun (Department of Food Science and Biotechnology of Animal Resources, Konkuk University) ;
  • Han, Doo-Jeong (Department of Food Science and Biotechnology of Animal Resources, Konkuk University) ;
  • Choi, Yun-Sang (Department of Food Science and Biotechnology of Animal Resources, Konkuk University) ;
  • Kim, Cheon-Jei (Department of Food Science and Biotechnology of Animal Resources, Konkuk University)
  • Published : 2007.08.31
Download PDF
⟨ Previous Next ⟩

Abstract

Pre-rigor bovine sternomandibularis muscles were frozen at 3 hr postmortem thawed at various temperatures (18, 2, and $-2^{\circ}C$), and then meat quality and sensory properties were compared with those in chilled muscle (control). The meat thawed at $18^{\circ}C$ had lower ultimate pH, water holding capacity, and sensory scores and higher muscle shortening, thaw drip loss, and shear values than those of the other samples. The samples thawed at $-2^{\circ}C$ had significantly lower muscle shortening and higher sensory scores in tenderness and juiciness than those thawed at 18 and $2^{\circ}C$. Muscle shortening, pH, WHC, shear values, and sensory properties were not significantly different between control and sample thawed at $-2^{\circ}C$. By holding at $-2^{\circ}C$, thaw shortening was prevented and tender meat comparable to the chilled meat was obtained. These results indicate that thaw shortening can be largely eliminated if the frozen pre-rigor muscle is thawed at $-2^{\circ}C$.

Keywords

References

  1. Cuthbertson A. Hot-processing meat. A review of the rationale and economic implication. pp. 61-82. In: Developments in Meat Science- 1. Lawrie RA (ed). Applied Science Publishers Ltd., London, UK (1980)
  2. Pisula A, Tyburcy A. Hot processing of meat. Meat Sci. 43: 125- 134 (Supplement 1) (1996) https://doi.org/10.1016/0309-1740(96)00060-5
  3. Marsh BB, Thompson JF. Rigor mortis and thaw rigor in lamb. J. Sci. Food Agr. 9: 417-424 (1958) https://doi.org/10.1002/jsfa.2740090707
  4. Davey GL, Gilbert KV. The effect of carcass posture on cold, heat, and thaw shortening in lamb. J. Food Technol. 8: 445-451 (1973) https://doi.org/10.1111/j.1365-2621.1973.tb01731.x
  5. Hamm R. Postmortem changes in muscle with regard to processing of hot-boned beef. Food Technol.-Chicago 36: 105-115 (1982)
  6. Xiong YL, Blanchard SP. Functional properties of myofibrillar proteins from cold-shortened and thaw rigor bovine muscles. J. Food Sci. 58: 720-723 (1993) https://doi.org/10.1111/j.1365-2621.1993.tb09343.x
  7. Smulders FJM, Marsh BB, Swartz DR, Russell RL, Hoenecke ME. Beef tenderness and sarcomere length. Meat Sci. 28: 349-363 (1990) https://doi.org/10.1016/0309-1740(90)90048-B
  8. Yu LH, Lee ES, Jeong JY, Paik HD, Choi JH, Kim CJ. Effects of thawing temperature on the physicochemical properties of pre-rigor frozen chicken breast and leg muscles. Meat Sci. 71: 375-382 (2005) https://doi.org/10.1016/j.meatsci.2005.04.020
  9. Dransfield E. Calpains from thaw rigor muscle. Meat Sci. 43: 311- 320 (1996) https://doi.org/10.1016/S0309-1740(96)00022-8
  10. Behnke JR, Fennema O, Cassens RG. Rates of postmortem metabolism in frozen animal tissues. J. Agr. Food Chem. 21: 5-11 (1973) https://doi.org/10.1021/jf60185a016
  11. Koohmaraie M, Doumit ME, Wheeler TL. Meat toughening does not occur when rigor shortening is prevented. J. Anim. Sci. 74: 2935-2942 (1996)
  12. Cross HR, West RL, Dutson TR. Comparisons of methods for measuring sarcomere length in beef semitendinosus muscle. Meat Sci. 5: 261-266 (1980) https://doi.org/10.1016/0309-1740(81)90016-4
  13. Voyle CA. Sarcomere length and meat quality. pp. 95-97. In: Proceedings 17th European Meeting of Meat Research Workers. September 6-10, University of Bristol, Bristol, England. The American Meat Science Association, Savoy, IL, USA (1971)
  14. Grau R, Hamm R. A simple method for the determination of water binding in muscles. Naturwissenschaften 40: 29-30 (1953) https://doi.org/10.1007/BF00595734
  15. Kim CJ, Lee ES. Effects of quality grade on the chemical, physical, and sensory characteristics of hanwoo (Korean native cattle) beef. Meat Sci. 63: 397-405 (2003) https://doi.org/10.1016/S0309-1740(02)00099-2
  16. SAS Institute, Inc. SAS User's Guide. Statistical Analysis Systems Institute, Cary, NC, USA (2003)
  17. Honikel KO, Kim CJ, Hamm R, Roncales P. Sarcomere shortening of prerigor muscles and its influence on drip loss. Meat Sci. 16: 267-277 (1986) https://doi.org/10.1016/0309-1740(86)90038-0
  18. Cornforth DP, Pearson AM, Merkel RA. Relationship of mitochondria and sarcoplasmic reticulum to cold shortening. Meat Sci. 4: 103- 121 (1980) https://doi.org/10.1016/0309-1740(80)90036-4
  19. Honikel KO, Roncales P, Hamm R. The influence of temperature on shortening and rigor onset in beef muscle. Meat Sci. 8: 221-241 (1983) https://doi.org/10.1016/0309-1740(83)90046-3
  20. Locker RH, Hagyard CJ. A cold shortening effect in beef muscles. J. Sci. Food Agr. 14: 787-793 (1963) https://doi.org/10.1002/jsfa.2740141103
  21. Hertzman C, Olsson U, Tornberg E. The influence of high temperature, type of muscle, and electrical stimulation on the course of rigor, ageing, and tenderness of beef muscles. Meat Sci. 35: 119- 141 (1993) https://doi.org/10.1016/0309-1740(93)90074-R
  22. Macfarlane JJ, Turner RH, Ratcliff D. Comparison of the effects of pre-rigor cold and pressure treatments on some properties of beef biceps femoris muscles. J. Food Sci. 41: 1447-1448 (1976) https://doi.org/10.1111/j.1365-2621.1976.tb01192.x
  23. Marsh BB, Carsens RG, Kauffman RG, Briskley EJ. Hot boning and pork tenderness. J. Food Sci. 37: 179-180 (1972) https://doi.org/10.1111/j.1365-2621.1972.tb03415.x
  24. Marsh BB, Leet NG. Studies in meat tenderness. The effects of cold shortening on toughness. J. Food Sci. 31: 450-459 (1966) https://doi.org/10.1111/j.1365-2621.1966.tb00520.x
  25. Hamm R, Deatherage FE. Changes in hydration, solubility, and charges of muscle proteins during heating of meat. Food Res. 25: 587-610 (1960) https://doi.org/10.1111/j.1365-2621.1960.tb00004.x
  26. Offer G, Knight P. The structural basis of water-holding in meat. Part 1. General principles and water uptake in meat processing. pp. 63-171. In: Developments in Meat Science-4. Elsevier Applied Science Publishing Co., Inc., New York, NY, USA (1988)
  27. Davey CL, Kuttel H, Gilbert KV. Shortening as a factor in meat aging. J. Food Technol. 2: 53-56 (1967) https://doi.org/10.1111/j.1365-2621.1967.tb01325.x
  28. Marsh BB, Leet NG, Dickson MR. The ultrastructure and tenderness of highly cold-shortened muscle. J. Food Technol. 9: 141-147 (1974) https://doi.org/10.1111/j.1365-2621.1974.tb01757.x