Enzyme activity and stability control by amphiphilic self-organizing systems in aqueous solutions

Abstract

The interaction of surfactants with proteins in aqueous solutions has been the subject of many investigations to understand the interactions between membrane proteins and lipids, structurally similar to synthetic surfactants. The effect of surfactant on enzyme structure and activity is the result of chemically selective interactions that may be influenced both by the enzyme structure and by the chemistry of the surfactant. For many years, surfactants have been considered as non-specific denaturants of proteins, even if in the literature several of them are reported to enhance activity and/or stability of some enzymes: the detergent can interact with the enzyme and cause a conformational change to a more active form and/or stabilize its native folded structure. Although the surfactant head group seems to have a determining role, other structural features of the detergent are also important in influencing the catalytic properties of an enzyme, i.e. head group size and its hydrophobic/hydrophilic balance. Up to now it is very difficult to predict the molecular features of the surfactant and an extensive investigation on the relationship between the surfactant chemical structure and the catalytic properties of enzyme is still required.