Oscillatory transverse electric field enhances mass transfer and protein capacity in ion-exchange electrochromatography

Tan, Guo-Min; Shi, Qinghong; Sun, Yan

doi:10.1016/j.chroma.2005.08.089

Cited by 9 publications

(9 citation statements)

References 34 publications

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“…From the figure, it can be seen that the DBC values of the two proteins in the pIEEC were both about 2.3 times higher than those in the IEC. This is a result similar to that obtained using BSA as a model protein [24]. Moreover, the flatter frontal analysis curves observed in the pIEEC than those in the IEC (Figs.…”

Section: ) By Comparison Of Figs 2supporting

confidence: 77%

“…The electric current was always kept constant at 30 mA. This electric field condition has proven to significantly increase the DBC of BSA [24]. All the feeding solutions were kept at 68C in the chromatographic processes.…”

Section: Chromatographic Systemmentioning

confidence: 99%

“…Previous work has proven that the pIEEC gave enhanced DBC for a pure protein (BSA) [24]. To examine if it is still true for a practical protein feedstock, frontal analysis chromatography was carried out with the crude HEW solution.…”

Section: Frontal Analysis With Crude Hew Solutionmentioning

confidence: 99%

“…Studies on the sizeexclusion chromatography of proteins with noncharged particles (Sephadex G-75) by this kind of electrochromatography have shown increased separation capability resulting from the electrophoresis migration and concentration polarization [22,23]. Moreover, the effect of electric field strength on the DBC of BSA was experimentally studied in this column packed with DEAE Sepharose Fast Flow as well [24]. The results indicated that it was the inter/intraparticle electrokinetic mass transport that made the DBC to increase linearly upon increasing the electric field strength, including both electro-osmosis and electrophoresis.…”

Section: Introductionmentioning

confidence: 99%

“…In this work, we focus on the separation of hen egg-white (HEW) proteins by the ion-exchange electrochromatography with an oscillatory electric field perpendicular to the mobile-phase flow driven by pressure (pIEEC [24]). HEW is a complicated protein mixture and is often used as a typical feedstock for studying anion-exchange chromatography [25].…”

Section: Introductionmentioning

confidence: 99%

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High‐capacity purification of hen egg‐white proteins by ion‐exchange electrochromatography with an oscillatory transverse electric field

Yuan

Zhao

Dong

et al. 2006

J of Separation Science

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Original PaperHigh-capacity purification of hen egg-white proteins by ion-exchange electrochromatography with an oscillatory transverse electric fieldThe ion-exchange electrochromatography with an oscillatory electric field perpendicular to the mobile-phase flow driven by pressure (pIEEC) was used to separate hen egg-white (HEW) proteins. The results were compared with those of normal ionexchange chromatography (IEC). The column was designed as three-compartment rectangular column of 2-mL with dimensions (length6width6depth) of 4061065 mm 3 and the electric field was applied across the direction of column width. Q Sepharose FF was packed into the central compartment as the chromatographic bed. It was confirmed that the dynamic binding capacity (DBC) of different proteins (ovotransferrin and ovalbumin) in the HEW solution increased 2.3 times when an oscillatory electric current of 30 mA at 1/20 Hz was applied in the transverse column direction. Then, the HEW proteins were separated by the pIEEC at loading amounts 2.3-fold higher than those by the IEC. When the feedstock of about one-third of the DBC was applied to the columns (i. e., 7 mL for the pIEEC and 3 mL for the IEC), similar separation efficiencies of the two chromatographic modes were achieved. Both the recovery yield and purity reached 73% to over 90%. The results indicate that the pIEEC is promising for high-capacity purification of proteins.

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Section: ) By Comparison Of Figs 2supporting

confidence: 77%

Section: Chromatographic Systemmentioning

confidence: 99%

Section: Frontal Analysis With Crude Hew Solutionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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High‐capacity purification of hen egg‐white proteins by ion‐exchange electrochromatography with an oscillatory transverse electric field

Yuan

Zhao

Dong

et al. 2006

J of Separation Science

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Protein adsorption‐dependent electro‐kinetic pore flow: Modeling of ion‐exchange electrochromatography with an oscillatory transverse electric field

et al. 2010

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Electro-kinetic acceleration of protein mass transfer was studied by dynamic chromatographic experiments and computer simulations on IEC with an oscillatory transverse electric field (EF) perpendicular to the mobile-phase flow (pIEEC). The breakthrough behavior of BSA was investigated at different electric current densities. A two-dimensional mathematical model has been established to describe the electro-kinetic convection-diffusion behavior of protein adsorption in a single adsorbent particle. The equation was coupled with the axial dispersion model to simulate the dynamic adsorption process in the pIEEC. The model parameters were determined by independent experiments or calculations. It was found that protein adsorption led to an exponential decrease of intraparticle electro-kinetic flow with increasing protein adsorption. Taking this effect into consideration, the model calculations could well describe dynamic breakthrough curves. Moreover, protein distribution in adsorbents was observed to present excursion along the periodical oscillatory EF direction. At the beginning of pIEEC, intraparticle convection caused by the EF contributed more to the enhancement of dynamic binding capacity. Finally, it was confirmed that both the EOF and electrophoresis contributed to the acceleration of mass transfer.

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Effect of electric field on the partitioning behavior of solutes in entropic interaction chromatography

Shi

Jia

et al. 2013

J. Sep. Science

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In this study, a novel column design with a round cross-section was proposed to be suitable for a transverse electric field (EF). Additionally, two beads for entropic interaction chromatography (EIC) were prepared by grafting glycidyl methacrylate onto Toyopearl HW-65F (T65F) beads. Solute partitioning was then investigated to elucidate the role of graft polymerization with and without an EF. In a T65F column, solute partitioning was attributed to the distinct pore structure in the beads and was governed by pore flow. Under EF, partition coefficients (Kp) for solutes decreased with increasing EF strength. In the two EIC columns, a decrease of Kp was also observed without an EF while the fractionation windows were extended. It was more pronounced in the EIC column with a high grafting density (T65F-H). This was explained by the decrease in the effective pore size of solutes caused by the steric hindrance of polymer chains. Under an EF, the solutes showed different partitioning behaviours in the T65F-H column. With increasing EF strength, Kp for vitamin B12 and myoglobin was decreased. In contrast, Kp for large solutes increased as a result of concentration polarization on the bead surface. Both behaviors were related to the modulation of graft polymerization to residual charge on the matrix and the pore size of the solutes.

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Oscillatory transverse electric field enhances mass transfer and protein capacity in ion-exchange electrochromatography

Cited by 9 publications

References 34 publications

High‐capacity purification of hen egg‐white proteins by ion‐exchange electrochromatography with an oscillatory transverse electric field

High‐capacity purification of hen egg‐white proteins by ion‐exchange electrochromatography with an oscillatory transverse electric field

Protein adsorption‐dependent electro‐kinetic pore flow: Modeling of ion‐exchange electrochromatography with an oscillatory transverse electric field

Effect of electric field on the partitioning behavior of solutes in entropic interaction chromatography

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