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Prevention of thaw-rigor during frozen storage of bigeye tuna Thunnus obesus and meat quality evaluation

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Abstract

Thaw-rigor is often found in frozen meat of bigeye tuna Thunnus obesus. Excessive amounts of drip loss and stiffness greatly lower the commercial value of tuna meat. In order to prevent thaw-rigor in meat stored at −60°C post-capture, we adapted a temperature shift technique that stores the meat at −7°C for 1 day or −10°C for 7 days before thawing. Biochemical changes in muscle of bigeye tuna before and after the temperature shift to −7 or −10°C were characterized. Contents of ATP, NAD+, glycogen, and creatine phosphate decreased after the temperature shift. NAD+ levels decreased faster than ATP levels and were highly correlated with the rigor index. Thaw-rigor occurred in muscle containing NAD+ at 1 μmol/g and ATP at 7 μmol/g. On the other hand, the meat color of tuna during frozen storage changed to brown depending on the storage temperature and reflected the rate of metmyoglobin (met-Mb) formation. Met-Mb formation increase was dependent on the decrease in NADH levels during the frozen storage. A temperature shift technique with storage at −7°C for 1 day or −10°C for 7 days before thawing prevented thaw-rigor and met-Mb formation.

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References

  1. Bito M (1978) Changes in NAD and ATP levels and pH in frozen-stored skipjack meat in relation to amount of drip. Bull Jpn Soc Sci Fish 44:897–902

    Article  CAS  Google Scholar 

  2. Bito M (1980) Effect of degradation of NAD and ATP in frozen-storage sardine meat on the changes of pH and amount of drip in the thawed meat. Bull Tokai Reg Fish Res Lab 103:65–72

    Google Scholar 

  3. Yamanaka H (1984) Influences of freezing rates on the extent of thaw rigor and glycolysis of carp muscle. Refrigeration 59:11–16

    CAS  Google Scholar 

  4. Matsumura F (2005) Regulation of myosin II during cytokinesis in higher eukaryotes. Trends Cell Biol 15:371–377

    Article  PubMed  CAS  Google Scholar 

  5. Farah CS, Reinach FC (1995) The troponin complex and regulation of muscle contraction. FASEB J 9:755–767

    PubMed  CAS  Google Scholar 

  6. Somlyo AP, Somlyo AV (2003) Ca2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase. Physiol Rev 83:1325–1358

    PubMed  CAS  Google Scholar 

  7. Adelstein RS, Conti MA (1975) Phosphorylation of platelet myosin increases actin-activated myosin ATPase activity. Nature 256:597–598

    Article  PubMed  CAS  Google Scholar 

  8. Bito M, Honma S (1967) Studies on the retention of meat color of frozen tuna-IV. Acceleration of discoloration of tuna meat by freezing and its relation to storage temperatures. Bull Jpn Soc Sci Fish 33:33–40

    Article  CAS  Google Scholar 

  9. Yamanaka H (1991) Rigor mortis in fish. Kouseisha Kouseikaku, Tokyo

    Google Scholar 

  10. Sellevold OF, Jynge P, Aarstad K (1986) High performance liquid chromatography: a rapid isocratic method for determination of creatine compounds and adenine nucleotides in myocardial tissue. J Mol Cell Cardiol 18:517–527

    Article  PubMed  CAS  Google Scholar 

  11. Cappeln G, Jessen F (2002) ATP, IMP, and glycogen in cod muscle at onset and during development of rigor mortis depend on the sampling location. J Food Sci 67:991–995

    Article  CAS  Google Scholar 

  12. Ehira S (1983) A study on enzymatic method for determining NAD and ATP in fish muscle. Bull Tokai Reg Fish Res Lab 109:57–76

    Google Scholar 

  13. Gerth A, Nieber K, Oppenheimer NJ, Hauschildt S (2004) Extracellular NAD+ regulates intracellular free calcium concentration in human monocytes. Biochem J 382:849–856

    Article  PubMed  CAS  Google Scholar 

  14. Ma LB, Yamanaka H, Ushio H, Watabe S (1992) Studies on the mechanism of thaw rigor in carp. Nippon Suisan Gakkaishi 58:1535–1540

    Article  Google Scholar 

  15. Kockskamper J, Zima AV, Blatter LA (2005) Modulation of sarcoplasmic reticulum Ca2+ release by glycolysis in cat atrial myocytes. J Physiol 564:697–714

    Article  PubMed  Google Scholar 

  16. O’Rourke B, Ramza BM, Marban E (1994) Oscillations of membrane current and excitability driven by metabolic oscillations in heart cells. Science 265:962–966

    Article  PubMed  Google Scholar 

  17. Huser J, Wang YG, Sheehan KA, Cifuentes F, Lipsius SL, Blatter LA (2000) Functional coupling between glycolysis and excitation-contraction coupling underlies alternans in cat heart cells. J Physiol 524:795–806

    Article  PubMed  CAS  Google Scholar 

  18. Xu KY, Zweier JL, Becker LC (1995) Functional coupling between glycolysis and sarcoplasmic reticulum Ca2+ transport. Circ Res 77:88–97

    PubMed  CAS  Google Scholar 

  19. Sitsapesan R, Williams AJ (1995) Cyclic ADP-ribose and related compounds activate sheep skeletal sarcoplasmic reticulum Ca2+ release channel. Am J Physiol 268:1235–1240

    Google Scholar 

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Acknowledgments

This study was supported by funds from Fisheries Research Agency. The authors thank Sumio Hirokawa, Ippei Fusejima, Hijiri Iga, Takayoshi Uehara, and Kosuke Yokota for kindly providing the tuna. We thank Masaki Kaneniwa for their useful discussions and technical support. We are very grateful to Michiaki Yamashita for critical reading of this manuscript and helpful comments.

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Correspondence to Shintaro Imamura.

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Imamura, S., Suzuki, M., Okazaki, E. et al. Prevention of thaw-rigor during frozen storage of bigeye tuna Thunnus obesus and meat quality evaluation. Fish Sci 78, 177–185 (2012). https://doi.org/10.1007/s12562-011-0427-7

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  • DOI: https://doi.org/10.1007/s12562-011-0427-7

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