Enzyme-responsive artificial chaperone system with amphiphilic amylose primer

Nobuyuki Morimoto, Naruhito Ogino, Tadashi Narita, Kazunari Akiyoshi

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)


An enzyme-responsive artificial chaperone system which employs an amphiphilic amylose primer (dodecyl maltopentaose, C12-MP) as a surfactant and phosphorylase b was designed to enable protein refolding. Effective refolding of carbonic anhydrase B after both heat denaturation (70 °C for 10 min) and guanidine hydrochloride (6 M) denaturation was observed by controlled association between the protein molecules and the C12-MP primer micelle through an enzymatic reaction.

Original languageEnglish
Pages (from-to)246-249
Number of pages4
JournalJournal of Biotechnology
Issue number3-4
Publication statusPublished - 2009 Mar 25
Externally publishedYes


  • Amylose
  • Artificial molecular chaperone
  • Enzymatic polymerizaion
  • Micelle
  • Protein refolding
  • Surfactant

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology


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