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  [in Japanese] Electric percolation phenomena and solubilization state of protein in reverse micellar organic media  [in Japanese]

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Author(s)

    • 直江 一光 NAOE Kazumitsu
    • 奈良工業高等専門学校物質化学工学科 Department of Chemical Engineering, Nara National College of Technology
    • 熊野 早紀 KUMANO Saki
    • 奈良工業高等専門学校物質化学工学科 Department of Chemical Engineering, Nara National College of Technology
    • 河越 幹男 KAWAGOE Mikio
    • 奈良工業高等専門学校物質化学工学科 Department of Chemical Engineering, Nara National College of Technology
    • 今井 正直 IMAI Masanao
    • 日本大学生物資源科学部食品科学工学科 Department of Food Science and Technology, College of Bioresource Sciences, Nihon University

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 <I>c</I> > 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 (Δ<I>T<SUB>p</SUB></I>) depended upon the solvent molecular volume and the protein species. In the case of lysozyme, Δ<I>T<SUB>p</SUB></I> increased with the molecular volume of solvent, while Δ<I>T<SUB>p</SUB></I> of cytochrome c showed the minimum value at the molecular volume of C8-9 alkane.

Journal

  • MEMBRANE

    MEMBRANE 26(2), 86-94, 2001-03-01

    THE MEMBRANE SOCIETY OF JAPAN

References:  43

Cited by:  1

Codes

  • NII Article ID (NAID)
    10008010403
  • NII NACSIS-CAT ID (NCID)
    AN0023215X
  • Text Lang
    JPN
  • Article Type
    Journal Article
  • ISSN
    03851036
  • NDL Article ID
    5724207
  • NDL Source Classification
    ZR2(科学技術--生物学--生化学)
  • NDL Call No.
    Z18-1127
  • Data Source
    CJP  CJPref  NDL  J-STAGE 
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