Effect of Glycolysis Rate in Porcine Muscle Postmortem on Gel Property of Pork Surimi

돼지 근육의 사후 해당속도가 돈육 수리미의 젤 특성에 미치는 영향

  • Kang Guen-Ho (Division of Animal Science and technology, College of Agriculture and Life Science, Gyeongsang National University) ;
  • Yang Han-Sul (Division of Animal Science and technology, College of Agriculture and Life Science, Gyeongsang National University) ;
  • Jeong Jin-Yeon (Division of Animal Science and technology, College of Agriculture and Life Science, Gyeongsang National University) ;
  • Joo Seon-Tea (Division of Animal Science and technology, College of Agriculture and Life Science, Gyeongsang National University) ;
  • Park Gu-Boo (Division of Animal Science and technology, College of Agriculture and Life Science, Gyeongsang National University)
  • 강근호 (경상대학교 동물자원과학부) ;
  • 양한술 (경상대학교 동물자원과학부) ;
  • 정진연 (경상대학교 동물자원과학부) ;
  • 주선태 (경상대학교 동물자원과학부) ;
  • 박구부 (경상대학교 동물자원과학부)
  • Published : 2005.12.01

Abstract

Properties of pant surimi derived from porcine longissimus muscle were investigated Rapid glycolysis of muscle reduced yield $\%$ of water-washed pork and moisture $\%$ of pent surimi because of ie lower ultimate pH. Gel Hardness was significantly (p<0.05) higher in pork surimi from rapid glycolysis muscle, but springiness was higher (p<0.05) in pork surimi from normal glycolysis muscle. SDS-PAGE pattern showed denaturation of sarcoplasmic proteins onto myofibrillar proteins in rapid glycolysis muscle, resulted in dark color and hard texture of pork surimi. Color and texture of gels were related with water-holding capacity of muscle proteins and moisture $\%$ in gel matrix. Results imply that glycolysis rate of porcine muscle at postmortem could affect gel properties of pork surimi, and muscle with rapid glycolysis muscle could produce a hard texture of pork surimi and dark color.

돈육을 수세하여 돈육 수리미를 제조할 때, 사후 해당 속도가 빠른 돈육을 원료육으로 이용하면 낮은 pH에 기인하여 보수성이 낮은 결과 적은 수분 함량을 보유하는 돈육 수세물을 획득하게 되어 수율이 낮아졌다. 사후 해당 속도가 빠른 돈육은 정상 돈육에 비해 육단백질의 변성이 유발되어 수분 함량이 낮고 치밀한 젤 매트릭스를 형성하여 경도가 높지만 탄력성이 낮은 돈육 수리미를 생산하였다. 뿐만 아니라 사후 해당 속도가 빠른 돈육은 변성된 근장 단백질이 근원섬유 단백질과 결합하여 수세되지 않고 돈육 수세물 내에 잔존하게 되어 돈육 수리미의 색깔을 어둡게 만드는 원인으로 작용한 것으로 사료된다.

Keywords

References

  1. Bendall, J. R. and Wismer-Pedersen, J. (1962) Some properties of the myofibrillar protein of normal and watery pork muscle. J. Food Sci. 27, 144-159 https://doi.org/10.1111/j.1365-2621.1962.tb00074.x
  2. Birth, G. S. (1978) The light scattering properties of foods. J. Food Sci. 43, 916-925 https://doi.org/10.1111/j.1365-2621.1978.tb02455.x
  3. Bourne, M. C. (1968) Texture profiling of ripening pears. J. Food Sci. 33, 223-226 https://doi.org/10.1111/j.1365-2621.1968.tb01354.x
  4. Camou, J. P. and Sebranek, J. G. (1991) Gelation characteristics of muscle protein from pale, soft, exudative (PSE) pork. Meat Sci. 30, 207-220 https://doi.org/10.1016/0309-1740(91)90067-Z
  5. Costa, L. M., Fiego, D. P. L., Dall'Olio, S., Davoli, R., and Russo, V. (2002) Combined effects of pre-slaughter treatments and lairage time on carcass and meat quality in pigs of different halothane genotype. Meat Sci. 61, 41-47 https://doi.org/10.1016/S0309-1740(01)00160-7
  6. Fischer, C., Hamm, R., and Honilkel, K. O. (1979) Changes in solubility and enzymatic activity of muscle glycogen phosphorylase in PSE muscle. Meat Sci. 3, 11-19 https://doi.org/10.1016/0309-1740(79)90020-2
  7. Gornall, A. G., Bardawill, C. J., and David, M. M. (1949) Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177, 751-766
  8. Ha, J. U., Woo, D. K., and Hwang, Y. M. (2000) Effect of carboxyl methyl cellulose and methyl cellulose on the functional properties of pork heart alginate/calcium(AC) surimi. Kor. J. Food Sci. Ani. Resour. 20, 199-206
  9. Helander, E. (1957) On quantitative muscle protein determination. Acta Physiologica Scandinavica, 41, 9-95
  10. Joo, S. T., Kauffman, R. G., Kim, B. C., and Kim, C. J. (1995) The relationship between color and water-holding capacity in postrigor porcine longissimus muscle. J. Muscle Foods. 6, 152-156
  11. Joo, S. T., Kauffman, R. G., Kim, B. C., and Park, G. B. (1999) The relationship of sarcoplasmic and myofibrillar protein solubility to colour and water-holding capacity in porcine longissimus muscle. Meat Sci. 52, 291-297 https://doi.org/10.1016/S0309-1740(99)00005-4
  12. Kang, G. H., Oh, S. H., Yang, H. S., Kim, J. S., Joo, S. T., and Park, G. B. (2003) Effect of myofibrillar protein extracted from pig hearts on quality characteristics of emulsion type sausages. Kor. J. Food Sci. Ani. Resour. 23, 122-127
  13. Laemmli, U. K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227, 680-685 https://doi.org/10.1038/227680a0
  14. Lanier, T. C. (1986) Functional properties of surimi. Food Technol. 40, 114-117
  15. Lan, Y. H., Novakofski, J., McCusker, R. H., Brewer, M. S., Carr, T. R., and McKeith, F. K. (1995) Thermal gelation properties of myofibrillar protein from pork, beef, fish, chicken and turkey muscles. J. Food Sci. 60, 936-940, 945 https://doi.org/10.1111/j.1365-2621.1995.tb06265.x
  16. Lee, S. K., Min, B. J., and Kang, C. G. (2001a) Effects of oleoresin spices on the quality of chicken surimi during frozen storage. Kor. J. Food Sci. Ani. Resour. 21, 292-299
  17. Lee, S. K., Min, B. J., and Kang, C. G. (2001b) Influence of propyl gallate, sodium ascorbate, and sodium tripolyphosphate on quality change of chicken surimi during storage. Kor. J. Anim. Sci. Technol. 43, 525-534
  18. Lesiow, T. and Xion, 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
  19. MacDougall, D. B. (1970) Characteristics of appearance of meat. I. The luminous absorbtion, scatter and internal transmittance of the lean of bacon manufactured from normal and pale pork. J. Sci. Food Agric. 21, 568-571 https://doi.org/10.1002/jsfa.2740211107
  20. Morioka, K. and Shimizu, Y. (1990) Contribution of sarcoplasmic proteins to gel formation of fish meat. Nippon Suisan Gakkaishi. 56, 929-933 https://doi.org/10.2331/suisan.56.929
  21. Okada, M. (1964) Effect of washing on the gelly forming ability of fish meat. Bulletin of the Japanese Society of Scientific Fisheries. 30, 255-261 https://doi.org/10.2331/suisan.30.255
  22. Okada, M. (1985) The history of surimi and surimi based products in JAPAN. Proceedings of the International Symposium on Engineered Seafood including Surimi, Seattle, pp. 30-31
  23. Owen, B. L., Montgomery, J. L., Ramsey, C. B., and Miller, M. F. (2000) Preslaughter resting and hot-fat trimming effects on the incidence of pale, soft and exudative (PSE) pork and han processing characteristics. Meat Sci. 54, 221-229 https://doi.org/10.1016/S0309-1740(99)00083-2
  24. Park, S., Brewer, M. S., Novakofski, J., Bechtel, P. J., and McKeith, F. K. (1996) Process and characteristics for a surimi-like material made from beef or pork. J. Food Sci. 61, 422-427 https://doi.org/10.1111/j.1365-2621.1996.tb14208.x
  25. SAS (2001) The SAS program for window. Cary, NC: The SAS Institute, Inc, USA
  26. Smith, D. M. (1988) Meat protein: functional properties in comminuted meat products. Food Technol. 23, 116-120
  27. Warner, R. D., Kauffman, R. G., and Greaser, M. L. (1997) Muscle protein changes postmortem in relation to pork quality traits. Meat Sci. 45, 339-352 https://doi.org/10.1016/S0309-1740(96)00116-7
  28. Xiong, Y. L. (1997) Structure-function relationships of muscle proteins: In Damodaran, S. and Paraf, A. (eds), Food proteins and their applications. New York, Marcel Dekker Inc. pp. 341-392
  29. Yasui, T., Ishioroshi, M., and Samejima, K. (1982) Effect of actomyosin on heat-induced gelation of myosin. Agric. Biol. Chem. 46, 1049-1059 https://doi.org/10.1271/bbb1961.46.1049
  30. Ziegler, G. R. and Foegeding, E. A. (1990) The gelation of proteins. Adv. Foods Res. Nutr. 34, 203-298 https://doi.org/10.1016/S1043-4526(08)60008-X