Enzyme-responsive artificial chaperone system with amphiphilic amylose primer

Nobuyuki Morimoto; Naruhito Ogino; Tadashi Narita; Kazunari Akiyoshi

doi:10.1016/j.jbiotec.2009.01.013

Enzyme-responsive artificial chaperone system with amphiphilic amylose primer

Nobuyuki Morimoto, Naruhito Ogino, Tadashi Narita, Kazunari Akiyoshi

Research output: Contribution to journal › Article › peer-review

26 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	246-249
Number of pages	4
Journal	Journal of Biotechnology
Volume	140
Issue number	3-4
DOIs	https://doi.org/10.1016/j.jbiotec.2009.01.013
Publication status	Published - 2009 Mar 25
Externally published	Yes

Keywords

Amylose
Artificial molecular chaperone
Enzymatic polymerizaion
Micelle
Protein refolding
Surfactant

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

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10.1016/j.jbiotec.2009.01.013

Cite this

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abstract = "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.",

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author = "Nobuyuki Morimoto and Naruhito Ogino and Tadashi Narita and Kazunari Akiyoshi",

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AU - Morimoto, Nobuyuki

AU - Ogino, Naruhito

AU - Narita, Tadashi

AU - Akiyoshi, Kazunari

N1 - Funding Information: This work was also supported by Grants-in-Aid for Scientific Research from the Japanese Government, and CREST, JST. Copyright: Copyright 2009 Elsevier B.V., All rights reserved.

PY - 2009/3/25

Y1 - 2009/3/25

N2 - 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.

AB - 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.

KW - Amylose

KW - Artificial molecular chaperone

KW - Enzymatic polymerizaion

KW - Micelle

KW - Protein refolding

KW - Surfactant

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Enzyme-responsive artificial chaperone system with amphiphilic amylose primer

Abstract

Keywords

ASJC Scopus subject areas

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