Electrostatic and Electrokinetic Interactions during Protein Transport through Narrow Pore Membranes

Pujar, Narahari S.; Zydney, Andrew L.

doi:10.1021/ie00034a032

Cited by 106 publications

(86 citation statements)

References 16 publications

(25 reference statements)

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“…8 Zeta potential of -20.0 mV for BSA and 7.7 mV for LF were obtained working with KCl and NaCl electrolytes at pH 7.0 being the difference of these values the highest observed. Under the selected conditions the separation BSA/LF by ultrafiltration using charged membranes is expected to be enhanced.…”

Section: Zeta Potential Measurementsmentioning

confidence: 88%

“…To maximize the effectiveness of the separation processes, an accurate description of the effect of physicochemical interactions between protein molecules is necessary [8]. Particle size measurements allow the correct selection of the membrane cut-off, as well as the proper prediction of protein aggregation and foaming, thus allowing for the correct selection of buffers, pH and temperatures for storage [7].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Accurate determination of key surface properties that determine the efficient separation of bovine milk BSA and LF proteins

Valiño

Román

Ibáñez

et al. 2014

Separation and Purification Technology

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. KeywordsDynamic light scattering, Zeta Potential, Bovine Serum Proteins, Bioprocess Design. AbstractThe aim of this work is to accurately measure fundamental surface properties, i.e., zeta potential, isoelectric point and protein size that determine the optimal separation conditions of Bovine serum albumin and lactoferrin, two high added value food proteins whose similarity in weight makes their separation a scientific and technical challenge.

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Section: Zeta Potential Measurementsmentioning

confidence: 88%

Section: Introductionmentioning

confidence: 99%

Accurate determination of key surface properties that determine the efficient separation of bovine milk BSA and LF proteins

Valiño

Román

Ibáñez

et al. 2014

Separation and Purification Technology

View full text Add to dashboard Cite

show abstract

“…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%

“…It was recognized that significant improvements in the ultrafiltration of the proteins can be obtained by controlling the pH and ionic strength of the protein solution. Pujar and Zydney (1994) found that the transmission of bovin serum albumin (BSA) through a 100 kDa membrane increased by more than two orders of magnitude as the salt concentration was increased from 1.5 mM to 150 mM [1]. This was attributed to the increased electrostatic exclusion of the charged BSA from the membrane pores at low ionic salt concentration.…”

Section: Introductionmentioning

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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“…Although ultrafiltration was originally viewed as a purely size-based exclusion phenomenon, it is now well established that protein transmission is strongly affected by electrostatic interactions between the charged protein and any charged groups on the polymer membrane. These effects can be quite dramatic, with the sieving coefficient reduced by more than 100-fold due as the salt concentration is lowered from 100 to 1 mM (Pujar and Zydney, 1994).…”

Section: Ultrafiltrationmentioning

confidence: 99%

Membrane technology for purification of therapeutic proteins

Zydney

2009

Biotech & Bioengineering

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Membrane systems are used throughout the downstream purification in the commercial production of high value therapeutic proteins. Over the last two decades, new membranes, modules, and systems have been developed specifically to meet the requirements of the biotechnology industry. These developments have been facilitated by an improved fundamental understanding of: (1) the effects of electrostatic interactions and concentration polarization on protein transmission during ultrafiltration and (2) the role of membrane morphology on protein fouling during both sterile and virus filtration. This perspective highlights some of the key work in this area and provides insights into possible future improvements in membrane technology for the purification of recombinant therapeutic proteins.

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Electrostatic and Electrokinetic Interactions during Protein Transport through Narrow Pore Membranes

Cited by 106 publications

References 16 publications

Accurate determination of key surface properties that determine the efficient separation of bovine milk BSA and LF proteins

Accurate determination of key surface properties that determine the efficient separation of bovine milk BSA and LF proteins

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

Membrane technology for purification of therapeutic proteins

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