The oxidative refolding of denatured-reduced lysozyme in the presence of cetyl trimethyl ammonium bromide (CTAB) and/or β -cyclodextrin ( β -CD) was investigated. The renaturation yield was improved in the presence of β -CD which inhibited the hydrophobic interaction between the unfolded protein molecules. However

β -CD concentration should be 3000-5000 times higher than the denatured enzyme to achieve a significant refolding effect. In contrast to β -CD

the refolding system with both CTAB and β -CD showed more favorable effect on the enzyme renaturation. With a properly enhanced guanidine hydrochloride concentration

the enzymatic activity of the denatured-reduced lysozyme could be completely regained. In addition

the optimal pH (8.5) and temperature (37℃) was established for the CTAB+ β -CD renaturation system.