Fisheries Science

, Volume 85, Issue 4, pp 757–765 | Cite as

Thermal stability of myosin and protective effect of F-actin on myosin affect the thermal inactivation of calcium-ATPase in unstable kuruma prawn myofibrils

  • Takayuki Sasaki
  • Masahito MatsukawaEmail author
Original Article Food Science and Technology


The thermal stability of myosin and the protective effect of F-actin on myosin in kuruma prawn myofibrils were investigated from the thermal inactivation rates at 25 °C of Ca-ATPase in myosin and myofibrils at various concentrations of KCl. The thermal inactivation rate constant (kD) of myofibrillar Ca-ATPase increased with increasing KCl concentration; however, the thermal inactivation followed a biphasic first-order reaction regardless of the KCl concentration: a relatively fast inactivation rate in the earlier phase (kDe) followed by a slower inactivation rate in the later phase (kDl) of the heat treatment. The thermal inactivation of myosin at various concentrations of KCl or sorbitol also followed a biphasic first-order reaction, and the differences between the kDe and kDl of myosin were always about twofold. kDe and kDl of myosin at 0.1 M KCl were decreased to 1/6 and 1/13, respectively, by the binding action of F-actin. These results suggest that the thermal stability of myosin and the protective effect of F-actin affect the stability and thermal inactivation of kuruma prawn myofibrils at physiological ionic strength.


Heat denaturation Potassium chloride Penaeidae Myofibrillar protein Myofibrillar denaturation Aquaculture Seafood Food quality 



  1. FAO (2016) FAO yearbook. Fishery and aquaculture statistics 2014. FAO, RomeGoogle Scholar
  2. Gomori G (1942) A modification of the colorimetric phosphorus determination for use with the photoelectric colorimeter. J Lab Clin Med 27:955–960Google Scholar
  3. Gornall AG, Bardawill CJ, David MM (1949) Determination of serum proteins by means of the biuret reaction. J Biol Chem 177:751–766Google Scholar
  4. Hamai M, Yamada-Orito M, Konno K (1991) Stabilization of fish myosin subfragment-1 by adenosine 5′-triphosphate and by sorbitol. Nippon Suisan Gakkaishi 57:747–753CrossRefGoogle Scholar
  5. Hashimoto A, Kobayashi A, Arai K (1982) Thermostability of fish myofibrillar Ca-ATPase and adaptation to environmental temperature. Bull Jpn Soc Sci Fish 48:671–684 (in Japanese with English abstract) CrossRefGoogle Scholar
  6. Jantakoson T, Thacaroj W, Konno K (2013) Myosin and actin denaturation in frozen stored kuruma prawn Marsupenaeus japonicus myofibrils. Fish Sci 79:341–347CrossRefGoogle Scholar
  7. Katoh N, Uchiyama H, Tsukamoto S, Arai K (1977) A biochemical study on fish myofibrillar ATPase. Bull Jpn Soc Sci Fish 43:857–867 (in Japanese with English abstract) CrossRefGoogle Scholar
  8. Koseki H, Kato S, Konno K (1993) Myosin extractability as a sensitive probe for the thermal denaturation of carp myofibrils. Nippon Suisan Gakkaishi 59:515–518 (in Japanese with English abstract) CrossRefGoogle Scholar
  9. Koyama H, Akolkar DB, Shiokai T, Nakaya M, Piyapattanakorn S, Watabe S (2012) The occurrence of two types of fast skeletal myosin heavy chains from abdominal muscle of kuruma shrimp Marsupenaeus japonicus and their different tissue distribution. J Exp Biol 215:14–21CrossRefGoogle Scholar
  10. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685CrossRefGoogle Scholar
  11. Matsukawa M, Arai K (1991) Dissociation and denaturation of walleye pollack myosin B induced by sodium pyrophosphate and MgCl2. Nippon Suisan Gakkaishi 57:1783–1788 (in Japanese with English abstract) CrossRefGoogle Scholar
  12. Murozuka T, Takashi R, Arai K (1976) Relative thermo-stabilities of Ca-ATPase of myosin and actomyosin from tilapia and rabbit. Bull Jpn Soc Sci Fish 42:57–63 (in Japanese with English abstract) CrossRefGoogle Scholar
  13. Ohno T, Kinoshita Y, Konno K (2011) Stabilizing effect of Ca2+ on myosin and myofibrils of squid mantle muscle as affected by heating conditions. Fish Sci 77:425–430CrossRefGoogle Scholar
  14. Sasaki T, Matsukawa M, Ooizumi T (2015) Thermal inactivation mode of myofibrillar Ca-ATPase of kuruma prawn Marusupenaeus japonicus. Nippon Suisan Gakkaishi 81:836–842 (in Japanese with English abstract) CrossRefGoogle Scholar
  15. Spudich JA, Watt S (1971) The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem 246:4866–4871Google Scholar
  16. Sriket P, Benjakul S, Visessanguan W, Kijiroongrojana K (2007) Comparative studies on chemical composition and thermal properties of black tiger shrimp (Penaeus monodon) and white shrimp (Penaeus vannamei) meats. Food Chem 103:1199–1207CrossRefGoogle Scholar
  17. Wakameda A, Nozawa S, Arai K (1983) Effect of neutral salts on thermal denaturation of myofibrillar Ca-ATPase of fish. Bull Jpn Soc Sci Fish 49:237–243 (in Japanese with English abstract) CrossRefGoogle Scholar
  18. Yuan C, Kaneniwa M, Wang X, Chen S, Cheng Y, Qu Y, Fukuda Y, Konno K (2006) Seasonal expression of 2 types of myosin with different thermostability in silver carp muscle (Hypophthalmichthys Molitrix). J Food Sci 71:C39–C43CrossRefGoogle Scholar

Copyright information

© Japanese Society of Fisheries Science 2019

Authors and Affiliations

  1. 1.Faculty of Marine BioscienceFukui Prefectural UniversityObamaJapan

Personalised recommendations