Development of Novel Molecular Assemblies that Enable High Selective Separation for Biomolecules

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Reversed micelles create unique environment in organic media. They are capable of solubilizing hydrophilic biomolecules (e.g., proteins, amino acids, DNA) in their aqueous interior. In the first study, we conducted protein extraction from an aqueous solution into isooctane using reversed micelles, and some important operational parameters to achieve an efficient protein transfer are elucidated. Targeted proteins were successfully extracted by reversed micelles that are formed by an anionic surfactant in isooctane. The degree of extraction of proteins was strongly influenced by the type of surfactant ih the organic solvent and ionic strength in the aqueous phase. The driving force of the protein transfer was electrostatic interaction between anionic surfactants and the positively charged protein. Anionic surfactants possessing two long-alkyl chains are the best candidate for the successful transfer of proteins from the aqueous solution to the reversed micellar solution.In the next study, novel function of reversed micelles as a protein refolding medium was carried out. In the reversed micellar phase, denatured proteins were completely reactivated in a nano-structured reversed micellar solution. This novel refolding technique facilitates a high renaturation yield at high protein concentration. The efficiency of protein refolding was enhanced when this novel technique by reversed micelles is applied to the solution containing higher protein concentration which, in the case of dilution method, would lead to protein aggregation. The reversed micellar technique is found to be a useful tool not only for protein separation but also for protein refolding.