Abstract
The extraction of bovine serum albumin (BSA) has been investigated using reverse micelles of hexadecyl trimethyl ammonium chloride/n-octanol/isooctane. Forward extraction process parameters such as the surfactant concentration, co-solvent concentration, pH, ionic strength, and species of the initial aqueous phase were important factors affecting the extraction performance. These parameters were varied to optimize the extraction efficiency. Under the optimized conditions, forward extraction efficiencies of BSA can reach practically 99.55%. The thermodynamic study revealed that the extraction of BSA is controlled by entropy changes. Maximum back-extraction efficiency of 85.16% can be obtained at low pH values and high salt concentrations. The structures of BSA during reverse micelle extraction did not change by comparing the circular dichroism spectra of BSA back-extracted to the aqueous phase with that of feed BSA.
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