Electric percolation phenomena and solubilization state of protein in reverse micellar organic media.

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  • Naoe Kazumitsu
    Department of Chemical Engineering, Nara National College of Technology
  • Matsumoto Chiharu
    Department of Chemical Engineering, Nara National College of Technology
  • Morii Seiji
    Department of Chemical Engineering, Nara National College of Technology
  • Kumano Saki
    Department of Chemical Engineering, Nara National College of Technology
  • Kawagoe Mikio
    Department of Chemical Engineering, Nara National College of Technology
  • Imai Masanao
    Department of Food Science and Technology, College of Bioresource Sciences, Nihon University

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Other Title
  • 逆ミセル有機溶媒における電気的パーコレーション現象とタンパク質の可溶化状態
  • ギャクミセル ユウキ ヨウバイ ニ オケル デンキテキ パーコレーション ゲンショウ ト タンパクシツ ノ カヨウカ ジョウタイ

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Abstract

Electric percolation phenomena of reverse micellar organic phase of sodium bis (2-ethylhexyl) sulfosuccinate (AOT) were investigated. Solubilization of electrolytes into the micellar water pool depressed the percolation between reverse micelles and increased the percolation temperature. In particular, caotropic GuHSCN and strong electrolyte KCl increased the percolation temperature more effectively. Solubilization of low-molecular-weight proteins into the micellar phase induced the percolation processes and lowered the percolation temperature, which was dependent on the protein concentration solubilized. The magnitude order of effectiveness of the protein on the percolation was cytochrome c > lysozyme > ribonuclease A. The efficiency of each protein in promoting percolation corresponded to its local solubilizing state in the micelles. In the cases of solubilizing both the electrolyte and the protein, the percolation processes were mutually affected by each additive. In the reverse micellar systems formed by different organic solvents (C6-10 alkane), the percolation temperature was linearly decreased with molecular volume of the solvent. The shift of the percolation temperature due to protein solubilization (ΔTp) depended upon the solvent molecular volume and the protein species. In the case of lysozyme, ΔTp increased with the molecular volume of solvent, while ΔTp of cytochrome c showed the minimum value at the molecular volume of C8-9 alkane.

Journal

  • MEMBRANE

    MEMBRANE 26 (2), 86-94, 2001

    THE MEMBRANE SOCIETY OF JAPAN

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