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Different effects of ionic and non-ionic compounds on the freeze denaturation of myofibrils and myosin subfragment-1

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Abstract

The effects of non-ionic (sorbitol, maltose, trehalose) and ionic compounds (Na-glutamate, Na-acetate, Na-sulfate, ammonium sulfate) on freeze denaturation of myosin subfragment-1 (S-1) and of myofibrils were compared. Sugars, Na-glutamate and Na-acetate well suppressed the freeze denaturation of myofibrils as well as S-1 in a concentration dependent manner. Although sulfate suppressed freeze denaturation of S-1 irregularly, it accelerated myofibril denaturation. It was concluded that sulfate salts were useless as cryoprotectant for myofibrils. Stabilization extent by F-actin in frozen storage was much less than that in heating.

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References

  1. Fukuda Y, Tarakita Z, Arai K. Effect of freshness of chum mackerel on the freeze-denaturation of myofibrillar protein. Nippon Suisan Gakkaishi 1984; 50: 845–852.

    CAS  Google Scholar 

  2. Matsumoto I, Arai K. Protective effect of sugar on freezedenaturation of carp myofibrillar protein. Nippon Suisan Gakkaishi 1985; 51: 833–839.

    CAS  Google Scholar 

  3. Matsumoto I, Arai K. Comparision of protective effects of several sugars on thermal and freeze denaturation of fish myofibrillar protein. Nippon Suisan Gakkaishi 1986; 42: 2633–2638.

    Google Scholar 

  4. Noguchi S, Matsumoto JJ. Studies on the control of the denaturation of fish muscle proteins during the frozen storage I. Preventive effect of Na-glutamate. Nippon Suisan Gakkaishi 1970: 36: 1078–1087.

    CAS  Google Scholar 

  5. Noguchi S, Matsumoto JJ. Studies on the control of the denaturation of fish muscle proteins during the frozen storage II. Preventive effect of amino acids and related compounds. Nippon Suisan Gakkaishi 1971; 37: 1115–1122.

    CAS  Google Scholar 

  6. MacDonald GA, Lanier TC, Swaisgood HE, Hamann DD. Mechanism for stabilization of fish actomyosin by sodium lactate. J. Agric. Food Chem. 1996; 44: 106–112.

    Article  CAS  Google Scholar 

  7. MacDonald GA, Lanier TC. Actomyosin stabilization to freeze-thaw and heat denaturation by lactate salts. J. Food Sci. 1994; 59: 101–105.

    Article  CAS  Google Scholar 

  8. Hayashi K, Konno K. Stabilization of myosin by ionic compounds as affected by F-actin. Fish. Sci. 2006; 72: 1306–1312.

    Article  CAS  Google Scholar 

  9. Katoh N, Uchiyama H, Tsukamoto S, Arai K. A biochemical study of fish myofibrillar ATPase. Nippon Suisan Gakkaishi 1977; 43: 857–867.

    CAS  Google Scholar 

  10. Konno K, Kato S, Eko M. Rapid method for isolation of myosin subfragment-1 from carp myofibrils. Nippon Suisan Gakkaishi 1990; 56: 1885–1890.

    CAS  Google Scholar 

  11. Murozuka T, Arai K. Purification and thermo-stability of myosin Ca-ATPase from the frozen muscle of yellowfin tuna. Nippon Suisan Gakkaishi 1976; 42: 65–70.

    CAS  Google Scholar 

  12. Sekine T, Takahashi S, Hikita S, Sutoh N, Satake K. Selective modification of myosin SH1 with 1,2,4-trinitrobenzene. VIII. Thiols of myosin. J. Biochem. 1984; 96: 27–33.

    PubMed  CAS  Google Scholar 

  13. Konno K. Suppressive effect of sulfate on fish myosin denaturation. Fish. Sci. 1998; 64: 848–849.

    CAS  Google Scholar 

  14. Konno K, Yamanodera K, Kiuchi H. Solubilization of fish muscle myosin by sorbitol. J. Food. Sci. 1997; 62: 980–984.

    Article  CAS  Google Scholar 

  15. Okada T, Ohta F, Inoue N, Akiba M. Denaturation of carp myosin B in KCl solution during frozen storage. Nippon Suisan Gakkaishi 1985; 51: 1887–1892.

    CAS  Google Scholar 

  16. Takatori K, Inoue N, Shinano H. Effect of KCl concentration and storage temperature on the denaturation of myosin B stored under unfrozen conditions at minus temperatures. Nippon Suisan Gakkaishi 1992; 58: 751–758.

    CAS  Google Scholar 

  17. Inoue N, Takatori K, Motoshige T, Shinano H. Effect of storage temperature on the freeze denaturation of fish myosin B. Nippon Suisan Gakkaishi 1992; 58: 2357–2360.

    CAS  Google Scholar 

  18. Hashimoto A, Kobayashi A, Arai K. Thermostability of fish myofibrillar Ca-ATPase and adaptation to environmental temperature. Nippon Suisan Gakkaishi 1982; 48: 671–684.

    CAS  Google Scholar 

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Authors and Affiliations

  1. Faculty of Fisheries Sciences, Hokkaido University, 041-8611, Hakodate Hokkaido, Japan

    Kumiko Hayashi, Yumiko Azuma, Satomi Koseki & Kunihiko Konno

  2. Department of Fisheries, School of Marine Science and Technology, Tokai University, 424-8610, Shimizu Shizuoka, Japan

    Satomi Koseki

Authors
  1. Kumiko Hayashi
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  2. Yumiko Azuma
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  3. Satomi Koseki
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  4. Kunihiko Konno
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Correspondence to Kunihiko Konno.

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Hayashi, K., Azuma, Y., Koseki, S. et al. Different effects of ionic and non-ionic compounds on the freeze denaturation of myofibrils and myosin subfragment-1. Fish Sci 73, 178–183 (2007). https://doi.org/10.1111/j.1444-2906.2007.01316.x

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  • DOI: https://doi.org/10.1111/j.1444-2906.2007.01316.x

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