Abstract
This contribution is concerned with the imidazolium-based ionic liquid surfactant being considered potential amphiphilic molecules. The interfacial dilational rheology of solutions of globular proteins (lysozyme and bovine serum albumin (BSA)) with imidazolium-based ionic liquid surfactant (1-dodecyl-3-methyl imidazolium bromide ([C12mim]Br)) have been measured as a function of the surfactant concentration, interface lifetime and interfacial pressure. The dynamic interfacial dilational modulus of lysozyme/[C12mim]Br solutions are always monotonous, but that of the BSA/[C12mim]Br solutions become nonmonotonous indicating the destruction of the protein structure. One can assume that some lysozyme molecules desorb from interface due to competitive of free [C12mim]Br molecules for lysozyme/[C12mim]Br solution with [C12mim]Br concentration increasing, however, BSA molecules unfolding of compact globule have been subject to conformational changes so that it can give space for more [C12mim]Br molecules to co-adsorb. This aimed to provide more theoretical information for practical applications of imidazolium-based ionic liquid surfactant.
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