Reversed micelles as novel protein refolding media

Masahiro Goto, Tsutomu Ono, Shintaro Furusaki

研究成果: Contribution to journalArticle


Refolding of denatured RNase A was conducted by a nanostructural surfactant-based molecular assembly formulated with sodium di-2-ethylhexyl sulfosuccinate (AOT) in isooctane. In the novel refolding technique, a solid-liquid extraction was utilized as an alternative to the ordinary protein extraction by reversed micelles based on a liquid-liquid extraction. The effects of operational parameters such as concentration of AOT, Wo (=[H2O]/[AOT]), and pH were examined on the solubilization of denatured proteins into a reversed micellar solution. The typically denatured form of the protein being isolated is reactivated due to its refolding ability within the confines of the reversed micelle medium. A complete renaturation of RNase A was accomplished by adjusting the composition of the redox reagent even at a high protein concentration in which protein aggregation would usually occur in aqueous media. In the final step, the renatured RNase A was effectively recovered from the reversed micellar solution without the loss of the enzymatic activity.

ジャーナルACS Symposium Series
出版物ステータス出版済み - 12 1 1999

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Chemical Engineering(all)

フィンガープリント Reversed micelles as novel protein refolding media' の研究トピックを掘り下げます。これらはともに一意のフィンガープリントを構成します。

  • これを引用

    Goto, M., Ono, T., & Furusaki, S. (1999). Reversed micelles as novel protein refolding media. ACS Symposium Series, 740, 374-383.