Affinity extraction of BSA by mixed reversed micellar system with unbound triazine dye

Abstract

The affinity extraction of proteins with unbound triazine dye in the mixed reversed micellar system has been studied. Bovine serum albumin (BSA) and Cibacron Blue 3GA (CB) were chosen, respectively, as a model protein and an unbound ligand. The affinity CB in the aqueous phase was directly transferred to the mixed reversed micelles formed with cationic surfactant cetyltrimethylammonium bromide (CTAB) and tributyl phosphate (TBP). The transfer of BSA to the reversed micelles increases significantly by the biospecific interaction with the addition of a small amount of CB to the aqueous phase. For solutions with pH < p I, the selectivity of proteins can be expected with the presence of affinity CB since no BSA was found to be extracted into the reverse micelles without the addition of CB. The BSA transfer to the reversed micelles increases significantly by the addition of TBP to the organic phase. Most of BSA (∼82%) extracted into the reversed micelles can be back extracted into the aqueous phase by the increase of n-hexanol concentration in the organic phase while no CB would be transferred into the stripping aqueous solution at the same time.