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Myosin and actin denaturation in frozen stored kuruma prawn Marsupenaeus japonicus myofibrils

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  • Food Science and Technology
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Abstract

Myosin and actin denaturation in kuruma prawn myofibrils stored frozen (0.1 M NaCl, pH 7.5) at −20 °C was investigated. The inactivation profile of Ca2+-ATPase in the myofibrils was identical to that for myosin, indicating that myosin in myofibrils was not protected by actin. The presence of myosin detached from actin in the soluble fraction was proven by ammonium sulfate fractionation in the absence and presence of Mg-ATP. Actin denaturation in myofibrils was further confirmed by its increased susceptibility to chymotryptic degradation. In the frozen myofibrils, actin denatured more rapidly quicker than myosin: actin had completely denatured by storage day 1, followed by a gradual denaturation of myosin. Both myosin and actin in the frozen stored myofibrils retained their high salt-solubility, which decreased slowly during the frozen storage period. The presence of aggregated inactivated myosin in the salt-soluble fraction was proven by precipitation at 40 % saturation of ammonium sulfate in the presence of Mg-ATP, leaving active monomeric myosin in the soluble fraction. Almost no actin denaturation was observed with heated myofibrils.

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Authors and Affiliations

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

    Thitima Jantakoson, Wichulada Thavaroj & Kunihiko Konno

  2. Faculty of Agricultural Technology, Songkhla Rajabhat University, Mueang Songkhla, Songkhla, 36000, Thailand

    Thitima Jantakoson

  3. Faculty of Liberal Arts, Rajamangala University of Technology Srivijaya, Mueang Songkhla, Lampang, 52000, Thailand

    Wichulada Thavaroj

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  1. Thitima Jantakoson
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  2. Wichulada Thavaroj
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  3. Kunihiko Konno
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Correspondence to Kunihiko Konno.

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Jantakoson, T., Thavaroj, W. & Konno, K. Myosin and actin denaturation in frozen stored kuruma prawn Marsupenaeus japonicus myofibrils. Fish Sci 79, 341–347 (2013). https://doi.org/10.1007/s12562-012-0589-y

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  • DOI: https://doi.org/10.1007/s12562-012-0589-y

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