Abstract
We present a review of recent theoretical and experimental work aimed at investigating the potential use of two-phase aqueous surfactant systems for the purification of hydrophilic proteins by liquid-liquid extraction techniques. The systems studied include (1) a two-phase aqueous nonionic surfactant (n-decyl tetra(ethylene oxide), C 10 E 4) system, and (2) a two-phase aqueous zwitterionic surfactant (dioctanoyl phosphatidylcholine, C 8-lecithin) system. The theoretical formulation assumes that excluded-volume interactions between the hydrophilic proteins and the surfactant micelles present in the solution play the dominant role in determining the experimentally observed partitioning behavior, and it incorporates (i) the self-assembling character of micelles, which allows them to grow into long, cylindrical microstructures with varying temperature and/or surfactant concentration, and (ii) a broad polydisperse distribution of micellar sizes. The theoretically predicted protein partitioning is compared with experimental measurements of the partitioning of several hydrophilic proteins, including cytochrome c, soybean trypsin inhibitor, ovalbumin, bovine serum albumin, and catalase, in two-phase aqueous C 10 E 4 and C 8-lecithin systems, and is found to be in good agreement. The results of this investigation suggest that two-phase aqueous surfactant systems of the type considered in this paper are potentially useful as extractant phases for the liquid-liquid extraction of proteins and other biomaterials.
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Liu, CL., Nikas, Y.J., Blankschtein, D. (1995). Two-Phase Aqueous Surfactant Systems for the Purification of Biomaterials. In: Rogers, R.D., Eiteman, M.A. (eds) Aqueous Biphasic Separations. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1953-9_4
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DOI: https://doi.org/10.1007/978-1-4615-1953-9_4
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