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

Liu, Chia-li; Kamei, Daniel T.; King, Jonathan; Wang, Daniel I. C.; Blankschtein, Daniel

doi:10.1016/s0378-4347(98)00013-9

Cited by 134 publications

(120 citation statements)

References 26 publications

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“…64,65 In these systems, an aqueous surfactant solution, under appropriate conditions, spontaneously separates into two predominantly aqueous, yet immiscible, liquid phases, one of which has a greater concentration of micelles than the other. 66 In recent times ATPMS have been investigated for possible industrial applications. Nonionic surfactants carrying ethylene oxide groups as hydrophilic moiety exhibit phase separation above a certain temperature.…”

Section: Aqueous Two-phase Micellar Systemsmentioning

confidence: 99%

Liquid–liquid extraction of biomolecules: an overview and update of the main techniques

Mazzola

Lopes

Hasmann

et al. 2007

J of Chemical Tech & Biotech

220

119

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Two-phase systems can be exploited in separation science for the extraction/purification of desired biomolecules. This article reviews recent experimental work on the use of aqueous two-phase polymer systems, two-phase aqueous micellar systems and reversed micellar systems for the extraction/purification of biomolecules. The experimental partitioning behavior of different biomolecules is reviewed and new results with nisin and lipopolysaccharides are presented. An extensive description of each system is presented, based on the biomolecules behavior and the tools employed to improve their extraction and purification.

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Section: Aqueous Two-phase Micellar Systemsmentioning

confidence: 99%

Liquid–liquid extraction of biomolecules: an overview and update of the main techniques

Mazzola

Lopes

Hasmann

et al. 2007

J of Chemical Tech & Biotech

220

119

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“…Based on this difference in the physicochemical environment of the two coexisting micellar phases, and since both micellar phases contain about or above 90 wt% of water, the two-phase aqueous nonionic C 10 E 4 micellar system provides a potential alternative for protein purification using principles of liquid-liquid extraction (Liu et al, 1996). Figure 3: Schematic illustration of phase separation in the aqueous C 10 E 4 micellar system upon increasing the temperature (Based on Liu et al, 1998). The C 10 E 4 micellar solution has a single phase at low temperatures and phase separates with an increase in temperature into a top, micellerich phase and a bottom, micelle-poor phase.…”

Section: Spherical Micelle Cylindrical Micelle Bilayermentioning

confidence: 99%

“…However, unlike the micelles present in the C 10 E 4 /buffer micellar system, every micelle in the two-phase aqueous C 10 E 4 /C 10 TAB/buffer micellar system is a mixed micelle composed of both C 10 E 4 and C 10 TAB, as shown schematically in : Schematic illustration of a net negatively charged hydrophilic protein (G6PD in the present case) partitioning in the two-phase aqueous mixed (C 10 E 4 /C 10 TAB) micellar system (Based on Liu et al, 1998). The black and white circles represent the hydrophilic heads of the C 10 E 4 and the C 10 TAB surfactant molecules, respectively.…”

Section: Spherical Micelle Cylindrical Micelle Bilayermentioning

confidence: 99%

Two-phase aqueous micellar systems: an alternative method for protein purification

Rangel-Yagui

Pessoa

Blankschtein

2004

Braz. J. Chem. Eng.

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-Two-phase aqueous micellar systems can be exploited in separation science for the extraction/purification of desired biomolecules. This article reviews recent experimental and theoretical work by Blankschtein and co-workers on the use of two-phase aqueous micellar systems for the separation of hydrophilic proteins. The experimental partitioning behavior of the enzyme glucose-6-phosphate dehydrogenase (G6PD) in two-phase aqueous micellar systems is also reviewed and new results are presented. Specifically, we discuss very recent work on the purification of G6PD using: i) a two-phase aqueous micellar system composed of the nonionic surfactant n-decyl tetra(ethylene oxide) (C 10 E 4 ), and (ii) a two-phase aqueous mixed micellar system composed of C 10 E 4 and the cationic surfactant decyltrimethylammonium bromide (C 10 TAB). Our results indicate that the two-phase aqueous mixed (C 10 E 4 /C 10 TAB) micellar system can improve significantly the partitioning behavior of G6PD relative to that observed in the two-phase aqueous C 10 E 4 micellar system.

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“…In these systems, an aqueous surfactant solution, under the appropriate solution conditions, spontaneously separates into two predominantly aqueous, yet immiscible, liquid phases, one of which has a greater concentration of micelles than the other (Liu et al, 1998;Rangel-Yagui et al, 2004). The difference between the physicochemical environments in the micelle-rich and in the micelle-poor phases forms the basis for an effective separation and makes ATPMS a convenient and potentially useful method for the separation, purification, and concentration of biomaterials (Liu et al, 1996;Dutra-Molino et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

Influence of salts on the coexistence curve and protein partitioning in nonionic aqueous two-phase micellar systems

Lopes

Santos-Ebinuma

Pessoa

et al. 2014

Braz. J. Chem. Eng.

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-Aqueous two-phase micellar systems (ATPMS) can be exploited in separation science for the extraction/purification of desired biomolecules. Prior to phase separation the surfactant solution reaches a cloud point temperature, which is influenced by the presence of electrolytes. In this work, we provide an investigation on the cloud point behavior of the nonionic surfactant C 10 E 4 in the presence of NaCl, Li 2 SO 4 and KI. We also investigated the salts' influence on a model protein partitioning. NaCl and Li 2 SO 4 promoted a depression of the cloud point. The order of salts and the concentration that decreased the cloud point was: Li 2 SO 4 0.5 M > NaCl 0.5 M ≈ Li 2 SO 4 0.2 M. On the other hand, 0.5 M KI dislocated the curve to higher cloud point values. For our model protein, glucose-6-phosphate dehydrogenase (G6PD), partitioning experiments with 0.5 M NaCl or 0.2 M Li 2 SO 4 at 13.85 °C showed similar results, with K G6PD ~ 0.46. The lowest partition coefficient was obtained in the presence of 0.5 M KI (K G6PD = 0.12), with major recovery of the enzyme in the micelle-dilute phase (%Recovery = 90%). Our results show that choosing the correct salt to add to ATPMS may be useful to attain the desired partitioning conditions at more extreme temperatures. Furthermore, this system can be effective to separate a target biomolecule from fermented broth contaminants.

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

Cited by 134 publications

References 26 publications

Liquid–liquid extraction of biomolecules: an overview and update of the main techniques

Liquid–liquid extraction of biomolecules: an overview and update of the main techniques

Two-phase aqueous micellar systems: an alternative method for protein purification

Influence of salts on the coexistence curve and protein partitioning in nonionic aqueous two-phase micellar systems

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