The feasibility of surfactant assisted refolding

which was performed by diluting denatured protein sample into a refolding buffer containing a surfactant of appropriate concentration

was examined by using recombinant human lysozyme (rhLys) and recombinant β-mannanase (rMan) as protein samples.The effectiveness of CTAB

an artificial chaperone consisting of CTAB and β-CD

as well as other kinds of surfactants was investigated respectively.The effects of these surfactants on refolding yield and product distribution were determined by using biological activity assay

non-reductive SDS-PAGE and fluorescence emission spectrometry. A significant increase in refolding yield occurred for rhLys when using CTAB and the artificial chaperone

compared to that obtained by using direct dilution. Moreover

the refolding of rhLys presented similar process characteristics to that of native lysozyme (Lys).In both cases

the yield and product distribution depended on the molar ratio of surfactant to protein. The artificial chaperone worked also for rMan

particularly at a high concentration of the denatured rMan. It was shown that the charge property and concentration of surfactant

and the concentration of protein being refolded are major parameters determining the success of refolding process. The results described above are helpful to both the understanding of process mechanism and the application of this new refolding method.