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.
- Artificial molecular chaperone
- Enzymatic polymerizaion
- Protein refolding
ASJC Scopus subject areas
- Applied Microbiology and Biotechnology