Role of electrostatic interactions during protein ultrafiltration

Rohani, Mahsa M.; Zydney, Andrew L.

doi:10.1016/j.cis.2010.07.002

Cited by 77 publications

(47 citation statements)

References 53 publications

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“…4. Assuming a continuous radial variation of the pore properties 29,30,33 would be more realistic for quantitative estimations but it is difficult in our case because of the limited microscopic information on the protein-pore surface interaction. Note also that eqn (3) is a crude estimation for the protein surface transport that oversimplifies the pore electrostatics and considers only the effect of the protein net charge.…”

Section: 19-25mentioning

confidence: 99%

“…More detailed microscopic models for the two-region pore and the electrostatic equations can be used at the price of increasing complexity. 20,29,30 In particular, Zydney and co-workers [30][31][32] have also identified the (protein charge)-(pore charge) interaction in the exponentials of eqn (3) as a crucial term in more rigorous models of protein ultrafiltration. Biesheuvel and co-workers 20 have analysed thoroughly protein adsorption and partition equilibrium in charged nanopores.…”

Section: 19-25mentioning

confidence: 99%

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Protein diffusion through charged nanopores with different radii at low ionic strength

Stroeve

Rahman

Naidu

et al. 2014

Phys. Chem. Chem. Phys.

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The diffusion of two similar molecular weight proteins, bovine serum albumin (BSA) and bovine haemoglobin (BHb), through nanoporous charged membranes with a wide range of pore radii is studied at low ionic strength. The effects of the solution pH and the membrane pore diameter on the pore permeability allow quantifying the electrostatic interaction between the charged pore and the protein.Because of the large screening Debye length, both surface and bulk diffusion occur simultaneously. By increasing the pore diameter, the permeability tends to the bulk self-diffusion coefficient for each protein.By decreasing the pore diameter, the charges on the pore surface electrostatically hinder the transport even at the isoelectric point of the protein. Surprisingly, even at pore sizes 100 times larger than the protein, the electrostatic hindrance still plays a major role in the transport. The experimental data are qualitatively explained using a two-region model for the membrane pore and approximated equations for the pH dependence of the protein and pore charges. The experimental and theoretical results should be useful for designing protein separation processes based on nanoporous charged membranes.

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Section: 19-25mentioning

confidence: 99%

Section: 19-25mentioning

confidence: 99%

Protein diffusion through charged nanopores with different radii at low ionic strength

Stroeve

Rahman

Naidu

et al. 2014

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

show abstract

“…This is attributed to the fact that, in the presence of salt the hydrophobic interactions between proteins and membrane can be decreased while the intra-hydrophobic interactions of the protein molecules can be significantly enhanced [34], moreover, the enlarged conformation of charged proteins becomes more compact due to the effect of ionic shielding [1,26,[35][36][37]. Additionally, the increase in ionic strength of the protein solution causes weakening of the electrostatic interaction between the protein and membrane, since the Na þ and Cl -ions decrease the activity coefficient of protonation at pH below the isoelectric points of myoglobin and lysozyme [32].…”

Section: Effect Of Ionic Strength Of the Protein Solution On Protein mentioning

confidence: 99%

“…The solution pH is an important parameter for the ultrafiltration of proteins through charged membranes [2,17,22,23,31,32]. The electrical charge on both the protein and the membrane changes with pH due to acidic/basic groups on the protein and the membrane surfaces.…”

Section: Effect Of Phmentioning

confidence: 99%

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Preparation and characterization of polyacrylonitrile membranes modified with polyelectrolyte deposition for separating similar sized proteins

Mahlicli

Altınkaya

Yürekli

2012

Journal of Membrane Science

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a b s t r a c tOne of the challenges faced by ultrafiltration membranes is to separate proteins with a small difference in their molecular weights. Recently, some researchers tried to overcome this problem by using charged membranes. This study examined the use of layer by layer deposition of polyelectrolytes on the chemically-modified polyacyronitrile membrane to increase the selectivity of the ultrafiltration. The membranes were prepared by wet-phase inversion technique and polyethylenimine (PEI) and alginate (ALG) were chosen as cationic and anionic polyelectrolytes for the modification of the surfaces. Sieving coefficient data were obtained with myoglobin and lysozyme as model proteins. The influences of solution pH, ionic strengths of the protein and polyelectrolyte solution and the number of polyelectrolyte bilayers on both selectivity and throughput were investigated. The highest selectivity and throughput were achieved with the 1-bilayer PEI-ALG coated polyacrylonitrile (PAN) membrane. Increasing the number of coating bilayers or the ionic strength of the protein solution or adding salt into the polyelectrolyte coating solution decreased both the maximum selectivity and throughput of the modified membranes.

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Ultrafiltration

Zydney

2018

Kirk-Othmer Encyclopedia of Chemical Technology

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Ultrafiltration is a pressure‐driven membrane process used extensively for protein concentration and desalting, for recovery and recycle of colloidal electropaints, and for removal of natural organic matter, color compounds, and viruses in wastewater treatment and the production of potable water. The performance of an ultrafiltration process is determined by the intrinsic properties of the ultrafiltration membrane, most significantly the permeability and selectivity, in combination with the effects of concentration polarization and fouling. This article reviews the key principles of ultrafiltration, including membrane casting, module design, and process configurations as well as a brief discussion of some of the more important industrial applications of ultrafiltration in bioprocessing, dairy systems, and water treatment.

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Role of electrostatic interactions during protein ultrafiltration

Cited by 77 publications

References 53 publications

Protein diffusion through charged nanopores with different radii at low ionic strength

Protein diffusion through charged nanopores with different radii at low ionic strength

Preparation and characterization of polyacrylonitrile membranes modified with polyelectrolyte deposition for separating similar sized proteins

Ultrafiltration

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