Journal
JOURNAL OF BIOTECHNOLOGY
Volume 140, Issue 3-4, Pages 246-249Publisher
ELSEVIER
DOI: 10.1016/j.jbiotec.2009.01.013
Keywords
Protein refolding; Artificial molecular chaperone; Surfactant; Amylose; Enzymatic polymerizaion; Micelle
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Funding
- Japanese Government
- CREST
- JST
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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 degrees 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. (C) 2009 Elsevier B.V. All rights reserved.
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