The synthesis of partially hydrophobic alpha-chymotrypsin is performed
in AOT reverse micelles to covalently bind hydrophobic molecules on t
he surface of the alpha-chymotrypsin. Fluorescence experiments indicat
e that the modified alpha-chymotrypsin is anchored on the inner surfac
e of the host reverse micelle. The structures of the microemulsions of
empty or filled reverse micelles are investigated by small-angle X-ra
y scattering, dynamic quasi-elastic light scattering, and conductivity
measurements. The corresponding intermicellar interactions are analyz
ed in terms of the adhesive hard sphere model. It is shown that neithe
r the presence nor the change in the location of the alpha-chymotrypsi
n modifies the intermicellar interactions and structure.