ACTIVITY AND CONFORMATION OF LYSOZYME IN REVERSED MICELLAR EXTRACTION

A study has been made on the activity and conformation of lysozyme in reversed micellar extraction using a spectrophotometer and spectropolarimeter, respectively. Lysozyme extracted in Aerosol OT/isooctane reverse micelle could be recovered into an aqueous solution in the pH range of 10.5-12 under conditions of high ionic strength. The enzyme activity of the lysozyme stripped to the aqueous solution of pH lower than 12 was retained as compared with the native enzyme. Circular dichroism spectra of lysozyme entrapped in the micelle showed that no significant change is observed in the structure of the main chain, although the fine structure originated from the aromatic residues is influenced by the surfactant molecules. In the stripping of lysozyme from the reverse micelle to aqueous solution, the enzyme is returned to the native conformation and thus remains the initial value in the activity.