Effect of ion binding on protein transport through ultrafiltration membranes

Menon, Manoj K.; Zydney, Andrew L.

doi:10.1002/(sici)1097-0290(19990505)63:3<298::aid-bit6>3.0.co;2-#

Cited by 32 publications

(6 citation statements)

References 37 publications

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“…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%

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%

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 feed-side pressure was maintained by nitrogen at 0.3 bar. To avoid concentration polarization, the feed solution was continuously stirred with a speed of 600 rpm [26]. To determine fouling tendency of the membranes, the cell was initially filled with water and the flux was measured.…”

Section: Ultrafiltration Studiesmentioning

confidence: 99%

“…As expected, the transmissions of both myoglobin and lysozyme through chemicallymodified, negatively charged PAN-C membrane increased with the increase in ionic strength. 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%

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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“…A large number of these studies have been devoted to the interaction of proteins with membranes in order to understand the adsorption mechanism through protein–membrane interactions. In such studies, many parameters constituting ionic environments such as pH, type and concentrations of ionic species, membrane hydrophilicity and protein concentration have been taken into account 5–8…”

Section: Introductionmentioning

confidence: 99%

Effects of ionic environment on the interfacial interactions between α‐amylase and polyether sulphone membranes

Salgın

2010

Surface & Interface Analysis

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This work reports a systematic study on the effects of ionic environment on the adsorption of α-amylase on 30 kDa polyether sulphone (PES) membranes on the basis of interfacial interaction of PES membrane and α-amylase enzyme in solution. Static adsorption of α-amylase was investigated at the solution pH values of pH = 4.5, 5.6 and 7.0; and for the ionic strengths of 0.001, 0.01 and 0.1 M KCl. The maximum adsorption occurred at the pH value below the isoelectric point (IEP) of the enzyme, whereas the minimum adsorption occurred at the IEP (pH = 5.6) of amylase. With increasing ionic strength, the adsorbed enzyme on the membrane decreased. The Freundlich and Langmuir adsorption models were used for the mathematical description of the adsorption equilibrium and isotherm constants were evaluated depending on ionic environment. To determine the steps affecting the adsorption mechanism, the experimental data were evaluated using pseudo-first-order and pseudo-second-order kinetic models. The experimental data fitted well the pseudo-first-order kinetics. To detect the structural changes which occurred, membrane surfaces were analyzed by FTIR-ATR spectroscopy. The effects of ionic environment on amylase activity were also investigated.

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Effect of ion binding on protein transport through ultrafiltration membranes

Cited by 32 publications

References 37 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

Effects of ionic environment on the interfacial interactions between α‐amylase and polyether sulphone membranes

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