The estimation of the hydrophobic and electrostatic contributions to the free energy change upon cationic surfactants binding to Jack bean urease.

The binding of a homologous series of n-alkyltrimethyl ammonium bromides with Jack bean urease (JBU) have been studied previously. It has been suggested that both electrostatic and hydrophobic interactions are involved in the formation of surfactant-protein complexes, but there is not any quantities analyzing method for resolution of their contributions in the process. In the present study, at first, the intrinsic Gibbs free energy of binding, DeltaG(b,nu), has been calculated for these systems and the trend of variation for both binding sets have been interpreted on basis of cooperativity and hydrophobicity of surfactants. Subsequently, a novel approach has been introduced for estimation of electrostatic and hydrophobic interactions in DeltaG(b,nu), by considering of this fact that DeltaG(b,nu) is the summation of electrostatic, DeltaG(b,nu)(ele), and hydrophobic, DeltaG(b,nu)(hyd), parts and considering this fact that just DeltaG(b,nu)(hyd) is a function of hydrocarbon tail length of surfactant (C(n)). The results represents the higher positive rule of electrostatic interactions in binding affinity of first set and inhibiting rule of this interaction in the second binding set. The predominate driving force in the second binding set is entropy statistical effect, which arises from numerous number of binding sites in this set. A binding mechanism on basis of structural changes in JBU due to its interaction with cationic surfactants has also been proposed.