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 lysozymewas used as a model protein and cetyltrimethylammonium bromide (CTAB) and-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.