Structural study of AOT reverse micelles containing native or modified proteins: influence of surfactant-enzyme interaction

✍ Scribed by M.P. Pileni; G. Cassin; F. Michel; F. Pitré

• Book ID: 103967628
• Publisher: Elsevier Science
• Year: 1995
• Tongue: English
• Weight: 856 KB
• Volume: 3
• Category: Article
• ISSN: 0927-7765
• DOI: 10.1016/0927-7765(94)01142-r

✦ Synopsis

In this paper, the solubilization effect of different proteins in sodium di(2-ethylhexyl)sulfosuccinate (AOT) reverse micelles is studied. From results obtained with chemically modified proteins, it is shown that the nature of the surfactant-protein interaction controls the intermicellar potential, not the location of the proteins within the droplets. By binding hydrophobic molecules onto the surface of ~-chymotrypsin and ribonuclease, we force these hydrophobic enzymes to interact, via hydrophobic forces, with the droplet's interface. Small-angle X-ray scattering (SAXS) and conductivity measurements suggest that modification of the intermicellar potential is not required when the enzymes are modified. Conversely, electrostatic forces play an important role, as is observed using cytochrome c and its derivatives differing in their superficial charge.