Survey of conditioning indicators for pork loins: Changes in myofibrils, proteins and peptides during postmortem conditioning of vacuum-packed pork loins for 30 days

Meat Science

Volumn 64, Issue 4, 2003, Pages 467-473

  Okumura, Tomoyuki ^a   Yamada, Ryoji ^a   Nishimura, Toshihide ^b  

^a NIPPON MEAT PACKERS INC   (Japan)

^b HIROSHIMA UNIVERSITY   (Japan)

Author keywords

Conditioning indicator; GAPDH; Peptide; Postmortem conditioning; Troponin T

Indexed keywords

PORK LOINS;

FOOD STORAGE; PROTEINS; VACUUM APPLICATIONS;

MEATS;

FOOD STORAGE; MEAT; PROTEINS; VACUUM;

EID: 0037208101     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0309-1740(02)00224-3     Document Type: Article

References (34)

1. Bucher, E. A., de la Brousse, F. C., & Emerson, C. P. (1989). Developmental and muscle-specific regulation of avian fast skeletal troponin T isoform expression by mRNA splicing. Journal of Biological Chemistry, 264, 12482-12491.
2. Cheng, C. S., & Parrish, F. C. Jr. (1978). Molecular changes in the salt-soluble myofibrillar proteins of bovine muscle. Journal of Food Science, 43, 461-463.
3. Davey, C. L., & Gilbert, K. V. (1969). Studies on meat tenderness. 7. Changes in the fine structure of meat during aging. Journal of Food Science, 34, 69-74.
4. Dransfield, E. (1994). Optimisation of tenderisation, ageing and tenderness. Meat Science, 36, 105-121.
5. Gahlmann, R., Troutt, A. B., Wade, R. P., Gunning, P., & Kedes, L. (1987). Alternative splicing generates variants in important functional domains of human slow skeletal troponin T. Journal of Biological Chemistry, 262, 16122-16126.
6. Herring, H. K., Cassens, R. G., & Briskey, E. J. (1965). Sarcomere length of free and restrained bovine muscle at low tempereature as related to tenderness. Journal of Science and Food Agriculture, 16, 379-385.
7. Hirano, M. (1992). Meat science. In S. Morita (Ed.), The science of meat and meat products (pp. 31-80). Japan: Sohbunsha Press (in Japanese).
8. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
9. Matsuishi, M. (1995). Meat flavor. Meat Science (Japanese meeting of meat research workers, Japan), 37, 183-198 (in Japanese).
10. Matsukura, U., Matsumoto, T., Tashiro, Y., Okitani, A., & Kalo, H. (1984). Morphological changes in myofibrils and glycerinated muscle fibers on treatment with cathepsins D and L. International Journal of Biochemistry, 16, 957-962.
11. Nakai, Y., Nishimura, T., Shimizu, M., & Arai, S. (1995). Effect of freezing on proteolysis of beef during storage at 4 °C. Bioscience, Biotechnology, and Biochemistry, 59, 2255-2258.
12. Negishi, H., Natsuno, M., & Yoshikawa, S. (1991). Certain physical and chemical properties in beef loin as indices of aging. Animal Science and Technology (Japan), 62, 1095-1103.
13. Negishi, H., Natsuno, M., & Yoshikawa, S. (1992). Shear force values, ATP-related compounds, myofibrillar fragmentation index and 30,000-dalton components in imported frozen beef loins as indices of aging. Animal Science and Technology (Japan), 63, 1267-1275.
14. Negishi, H., Yamamoto, E., & Kuwata, T. (1996). The origin of the 30 kDa component appearing during post-mortem ageing of bovine muscle. Meat Science, 32(3), 289-303.
15. Negishi, H., & Yoshikawa, S. (1993). The effects of beef muscle variety on beef aging indices. Animal Science and Technology (Japan), 64, 1168-1177.
16. Negishi, H., & Yoshikawa, S. (1994). Relationship between 30 kDa components and K-values in Broiler meat during postmortem storage. Animal Science and Technology (Japan), 62, 882-889.
17. Nishimura, T., Rhue, M. R., Okitani, A., & Kato, H. (1988). Components contributing to the improvement of meat taste during storage. Agricultural and Biological Chemistry, 52, 2323-2330.
18. Okayama, T., Fukumoto, H., Nakagawa, S., Yamanoue, M., & Nishikawa, I. (1992). Changes in protein content in subcellular sarcoplasmic fractions of muscles during conditioning of Japanese black cattle. Animal Science and Technology (Japan), 63, 855-860.
19. Okumura, T., Inuzuka, Y., Nishimura, T., & Arai, S. (1996). Changes in sensory, physical and chemical properties of vacuum-packed pork loins during the prolonged conditioning at 4 °C. Animal Science and Technology (Japan), 67, 360-367.
20. Olson, D. G., & Parrish, F. C. Jr. (1977). Relationship of myofibril fragmentation index to measures of beefsteak tenderness. Journal of Food Science, 42, 506-509.
21. Olson, D. G., Parrish, F. C. Jr., Dayton, W. R., & Goll, D. E. (1977). Effects of postmortem storage and calcium activated factors on the myofibrillar proteins of bovine skeletal muscle. Journal of Food Science, 42, 117-124.
22. Olson, D. G., Parrish, F. C. Jr., & Storomer, M. H. (1976). Myofibril fragmentation and shear resistance of three bovine muscles during postmortem storage. Journal of Food Science, 41, 1036-1041.
23. Parrish, F. C. Jr., Selvig, R. D., Culler, R. D., & Zeece, M. G. (1981). CAF activity, calcium concentration, and the 30,000-dalton component of tough and tender bovine longissmus muscle. Journal of Food Science, 46, 308-311.
24. Parrish, F. C. Jr., Young, R. B., Miner, B. E., & Andersen, L. D. (1973). Effects of postmortem conditions on certain chemical, morphological and organoleptic properties of bovine muscles. Journal of Food Science, 38, 690-695.
25. Pearlstone, J. R., Johnson, P., Carpenter, M. R., & Smillie, L. B. (1977). Primary structure of rabbit skeletal muscle troponin-T. Sequence determination of the NH2-terminal fragment CB3 and the complete sequence of troponin-T. Journal of Biological Chemistry, 252, 983-989.
26. Penny, I. F., & Dransfield, E. (1979). Relationship between toughness and troponin T in conditioned beef. Meat Science, 3, 1 35-141.
27. Samejima, K., & Wolfe, F. H. (1976). Degradation of myofibrillar protein components during postmortem aging of chicken muscle. Journal of Food Science, 41, 250-254.
28. Shimada, K., An, T., & Takahashi, K. (1998). Liberation of phospholipids from Z-disks of chicken skeletal muscle myofibrils by 0.01 mM calcium ions: weakening mechanism for Z-disks during postmortem aging of meat. Bioscience, Biotechnology, and Biochemistry, 62, 919-926.
29. Smillie, L. B., Golosinska, K., & Reinach, F. C. (1988). Sequences of complete cDNAs encoding four variants of chicken skeletal muscle troponin T. Journal of Biological Chemistry, 263, 18816-18820.
30. Smith, G. C., Culp, G. R., & Carpenter, Z. L. (1978). Postmortem aging of beef carcasses. Journal of Food Science, 43, 823-826.
31. Stoeva, S., Byrne, C. E., Mullen, A. M., Troy, D. J., & Voelter, W. (2000). Isolation and identification of proteolytic fragments from TCA soluble extracts of bovine M. longissimus dorsi. Food Chemistry, 69, 365-370.
32. Takahashi, K., Fukuzawa, T., & Yasui, T. (1967). Formation of myofibrillar fragments and reversible contraction of sarcomeres in chicken pectoral muscle. Journal of Food Science, 32, 409-413.
33. Watanabe, K., & Sato, Y. (1974). Meat flavor. Animal Science and Technology (Japan), 45, 113-128.
34. Wolfe, F. H., & Samejima, K. (1976). Further studies of postmortem aging effects on chicken actomyosin. Journal of Food Science, 41, 244-249.