Using bovine serum albumin (BSA) as a model protein, protein transport betw
een an aqueous phase and a reversed micellar organic phase was examined. Fr
om near-infrared spectra and UV absorption spectra, it was confirmed that C
TAB (cetyl trimethyl ammonium bromide)/hexanol-octane reversed micellar sol
ution is a suitable medium for BSA solubilization. It seems that the forwar
d transfer efficiency depends not only on the parameters of the two phases
(for example: the pH value, the concentration and species of ions in the aq
ueous phase, the content of surfactant and co-solvent in reversed micellar
solution), but also the titration behaviour and the concentration of the pr
otein in aqueous phase. The experimental results lead to the conclusion tha
t the major driving force in the protein extraction is electrostatic intera
ction. A modified phenomenological thermodynamic model for reversed micella
r extraction was presented, and shown to correlate the data on extraction e
fficiency of BSA with both pH value and surfactant concentration. The effec
ts of various factors, such as pH, and the type and concentration of salt i
n stripping solution, on BSA back transfer were also studied. It was found
that the backward transfer efficiency of BSA is strongly influenced by the
type of ions in stripping solution. When the operation runs under optimized
conditions and with suitable phase ratio, the recovery and concentration o
f protein were successfully obtained: In addition, the problems how long th
e reversed micellar solutions can be recycled and how much of the surfactan
t will be lost to the aqueous phase have been examined. (C) 1998 Elsevier S
cience S.A.