STRUCTURAL STUDY OF AOT REVERSE MICELLES CONTAINING NATIVE AND MODIFIED ALPHA-CHYMOTRYPSIN

The synthesis of partially hydrophobic alpha-chymotrypsin is performed in AOT reverse micelles to covalently bind hydrophobic molecules on the surface of the alpha-chymotrypsin. Fluorescence experiments indicate that the modified alpha-chymotrypsin is anchored on the inner surface of the host reverse micelle. The structures of the microemulsions of empty or filled reverse micelles are investigated by small-angle X-ray scattering, dynamic quasi-elastic light scattering, and conductivity measurements. The corresponding intermicellar interactions are analyzed in terms of the adhesive hard sphere model. It is shown that neither the presence nor the change in the location of the alpha-chymotrypsin modifies the intermicellar interactions and structure.