Refolding of denatured lysozyme assisted by artificial chaperones in reverse micelles

Abstract

This article reports oxidative protein refolding assisted by artificial chaperones in reverse micelles formed by nonionic surfactant of sorbitan trioleate modified with Cibacron Blue F-3GA in n-hexane. The denatured/reduced lysozyme was used as a model protein and cetyltrimethylammonium bromide (CTAB) and β-cyclodextrin as the artificial chaperones. The use of the artificial chaperones has proved to increase the refolding efficiency of denatured–reduced lysozyme at the concentration range studied (3.5–5.9 mg/mL). Moreover, the artificial chaperones increased the refolding yield in a wide range of urea concentrations. However, the optimal urea concentration range was little affected by the presence of the artificial chaperones.