Electrochemical Aspects of the Reverse Micelle Extraction of Proteins

Osakai, Toshiyuki; Shinohara, Aya

doi:10.2116/analsci.24.901

Cited by 14 publications

(18 citation statements)

References 39 publications

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“…The direct determination of proteins can be achieved to some extent with this approach, for example leading to detection of albumin [18] and a range of other proteins [25,26]. However, improved detection limits are achieved by exploiting the fact that proteins adsorb at the interface as a protein-organic anion complex.…”

Section: Proteins At the Itiesmentioning

confidence: 99%

Electrochemistry of proteins at the interface between two immiscible electrolyte solutions

Arrigan

Hackett

Mancera

2018

Current Opinion in Electrochemistry

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The electrochemistry of proteins at the interface between two immiscible electrolyte solutions (ITIES) is discussed, with detection capabilities based on proteinfacilitated anion transfer, and which has enabled protein detection via adsorptive stripping voltammetry. Targeting an enzymatic biomarker has achieved detection at picomolar concentrations, whilst studies into structural aspects of proteins at the ITIES have revealed formation of oligomers (cytochrome c) and unfolded protein (lysozyme) together with alterations to the protein secondary structures.

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Section: Proteins At the Itiesmentioning

confidence: 99%

Electrochemistry of proteins at the interface between two immiscible electrolyte solutions

Arrigan

Hackett

Mancera

2018

Current Opinion in Electrochemistry

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“…Osakai et al used surfactants in the organic phase as the basis for protein detection and found that cytochrome c could be transferred across the ITIES [33][34][35]. A range of proteins have been studied at the ITIES in the absence of surfactants and it was found that the proteins did not transfer across the ITIES but adsorbed there and facilitated the transfer of the organic anion to the aqueous phase [24,[26][27][28].…”

Section: Introductionmentioning

confidence: 99%

Electrochemical behaviour of myoglobin at an array of microscopic liquid–liquid interfaces

O'Sullivan

Arrigan

2012

Electrochimica Acta

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Electrochemistry at liquid-liquid interfaces, or at interfaces between two immiscible electrolyte solutions (ITIES), provides a basis for the non-redox detection of biological molecules, based on iontransfer or adsorption processes. The electroactivity of myoglobin at an array of micron-sized liquidorganogel interfaces was investigated. The µITIES array was patterned with a silicon membrane consisting of an array of eight pores with radii of ~12.8 µm and a pore to pore separation of ~400 µm.Using cyclic voltammetry at the ITIES, the protein was shown to adsorb at the interface and facilitate the transfer of the organic phase electrolyte anions to the aqueous side of the interface. The electrochemical current response was linear with concentration in the range of 1 -6 µM, with corresponding surface coverage of 10 -50 pmol cm -2 . The reverse peak currents was found to be proportional to the voltammetric scan rate, indicating a desorption process. The detection of the protein was only possibly when the pH of the aqueous phase solution was below the pI of the protein. The steady-state simple ion transfer behaviour of tetraethylammonium cation was decreased on the forward sweep, providing a qualitative indication of the presence of adsorbed protein at the interface.Increasing the ionic strength of the aqueous phase resulted in enhanced peak currents, possibly due to aggregation of protein precipitates in the aqueous solution. UV/Vis absorbance spectroscopy was used 1 ISE Member.2 | P a g e to investigate the effects of various aqueous electrolyte solutions on the structure of the protein, and it was shown that at low pH the protein is at least partially denatured. These results provide the basis for label-free detection of myoglobin at the ITIES.

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“…In addition, the reverse micelle solvent system is another ATPE that can be used as an alternative technique for protein separation due to its simplicity and feasibility of large-scale sample loading [94]. The reverse micelle solvent system is a very attractive system for protein separation [95,96]. Lastly, there is an application of a novel continuous ATPE prototype for the recovery of biomolecules [97].…”

Section: Recent Process In Atpe Applications Economic Costsmentioning

confidence: 99%

Aqueous Two-Phase Extraction Advances for Bioseparation

Goja¹,

Yang

Cui³

et al. 2013

J Bioproces Biotechniq

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Aqueous two-phase extraction (ATPE), unique liquid-liquid extraction, involves a transfer of solute from one aqueous phase to another. ATPE includes polymer-polymer type and polymer-salt type systems for the recovery of proteins. The protein must be recovered in a highly purified form in order to improve its quality, decrease energy consumption, reduce waste and minimize costs. To acquire the high value and achieve good control over processes, the reliable, multi-component products are required especially those with the ability to investigate complex processing conditions. The current reviewing paper discusses the most recent progresses for the recovery of biomolecules by using the ATPE, covering the mechanism, which controls the phase formation and the behavior of solute partitioning in aqueous twophase systems (ATPS) processes. The review discusses also the increasing application for the recovery of high-value bioproducts, the recent development of alternative low cost ATPS and disadvantages attributed to ATPS.

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Electrochemical Aspects of the Reverse Micelle Extraction of Proteins

Cited by 14 publications

References 39 publications

Electrochemistry of proteins at the interface between two immiscible electrolyte solutions

Electrochemistry of proteins at the interface between two immiscible electrolyte solutions

Electrochemical behaviour of myoglobin at an array of microscopic liquid–liquid interfaces

Aqueous Two-Phase Extraction Advances for Bioseparation

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