Effect of KCI on thermal gelation of fish myosin solutions

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  • Ooi Kazuko
    Department of Biological and Chemical Engineering, Faculty of Engineering, Gunma University
  • Kondo Shingo
    Department of Biological and Chemical Engineering, Faculty of Engineering, Gunma University
  • Takeno Hiroyuki
    Department of Biological and Chemical Engineering, Faculty of Engineering, Gunma University
  • Kikuchi Noriaki
    Department of Biological and Chemical Engineering, Faculty of Engineering, Gunma University
  • Terao Ken
    Department of Biological and Chemical Engineering, Faculty of Engineering, Gunma University
  • Dobashi Yoshiaki
    Department of Biological and Chemical Engineering, Faculty of Engineering, Gunma University
  • Ichikawa Hisashi
    Division of Advanced Materials, Graduate School of Science and Engineering, Nagasaki University

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  • Effect of KCl on Thermal Gelation of Fish Myosin Solutions

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Thermally induced gelation of white croaker myosin solutions was studied by means of circular dichroism (CD) and viscoelasticity measurements both in heating and cooling processes at different KCl concentrations of the medium. In the heating process, the α-helix content decreased steeply around 30°C, irrespective of KCl concentration. In the cooling process for the heated sample, it increased around the same temperature but did not return to the initial value at low temperatures, especially at low KCl concentration. In the first heating process, around 32°C, G and η increased at high KCl concentrations of 0.3M and 0.6M, whereas they decreased sharply at 0.2M KCl. This characteristic temperature effect shifts to the higher side at 0.12M KCl. In the second cooling process, G and η increased with larger slopes from 40°C at 0.3M and 0.6M KCl, whereas no clear change in the slope was found at 0.2M and 0.12M KCl because of data fluctuations due to the inhomogeneity of the sample. From these experimental results, it was suggested that the gelation of myosin solutions at the physiological KC1 concentration occurs by refolding myosin molecules once heated, but the network structure is inhomogeneous because of restricted unfolding in the heating process..

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