Separation of proteins and viruses using two-phase aqueous micellar systems

We discuss the utilization of a novel two-phase aqueous nonionic micellar system for the purification and concentration of biomolecules, such as proteins and viruses, by liquid–liquid extraction. The nonionic surfactant n-decyl tetra(ethylene oxide), C 10E 4, phase separates in water into two coexis...

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Bibliographic Details
Published in:Journal of chromatography. B, Biomedical sciences and applications Vol. 711; no. 1; pp. 127 - 138
Main Authors: Liu, Chia-li, Kamei, Daniel T, King, Jonathan A, Wang, Daniel I.C, Blankschtein, Daniel
Format: Journal Article
Language:English
Published: Netherlands Elsevier B.V 26-06-1998
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Summary:We discuss the utilization of a novel two-phase aqueous nonionic micellar system for the purification and concentration of biomolecules, such as proteins and viruses, by liquid–liquid extraction. The nonionic surfactant n-decyl tetra(ethylene oxide), C 10E 4, phase separates in water into two coexisting aqueous micellar phases by increasing temperature. The mild interactions of the C 10E 4 nonionic surfactant with biomolecules, combined with the high water content of the two coexisting micellar phases, suggest the potential utility of two-phase aqueous C 10E 4 micellar systems for the purification and concentration of biomolecules. In this paper, we review our recent experimental and theoretical studies involving the partitioning of several water-soluble proteins, including cytochrome c, soybean trypsin inhibitor, ovalbumin, bovine serum albumin, and catalase, in the two-phase aqueous C 10E 4 micellar system. In addition, we present results of our preliminary experimental investigation on the partitioning of bacteriophages, including φX174, P22, and T4.
ISSN:0378-4347
1387-2273
DOI:10.1016/S0378-4347(98)00013-9