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Enzyme-responsive artificial chaperone system with amphiphilic amylose primer

2009; Elsevier BV; Volume: 140; Issue: 3-4 Linguagem: Inglês

10.1016/j.jbiotec.2009.01.013

1873-4863

Nobuyuki Morimoto, Naruhito Ogino, Tadashi Narita, Kazunari Akiyoshi,

Enzyme Structure and Function

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.