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 10min) and guanidine hydrochloride (6M) denaturation was observed by controlled association between the protein molecules and the C12-MP primer micelle through an enzymatic reaction.
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