Concentration and desalination of protein solutions by ultrafiltration

Noordman, T.R.; Ketelaar, Thomas; Donkers, F.; Wesselingh, J.A.

doi:10.1016/s0009-2509(01)00403-1

Cited by 38 publications

(29 citation statements)

References 22 publications

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“…It has been demonstrated that the Maxwell-Stephan theory can provide the most general approach to describe the mass transfer in the concentration polarization layer in protein ultrafiltration if the protein properties can be well defined (Krishna and Wesselingh, 1997;Bellara and Cui, 1998). By taking into account electrostatic effects and nonidealities, this approach has been successful in predicting the effects of ionic strength and pH on permeate flux and rejections of small ions in protein ultrafiltration systems (Wesselingh and Vonk, 1995;Noordman et al, 2002). For a given protein separation system, if the properties of proteins can be well defined and the protein-protein interactions can be quantified, it is also feasible to use this approach to model the transport of proteins and small ions as well.…”

Section: Effects Of Stirring Speed and Permeate Fluxmentioning

confidence: 99%

Fractionation of bovine serum albumin and monoclonal antibody alemtuzumab using carrier phase ultrafiltration

Wang

Ghosh

Hale

et al. 2005

Biotech & Bioengineering

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Protein transmission and hence selectivity of separation can be significantly affected by solution pH and ionic strength in protein fractionation using ultrafiltration. Using parameter scanning ultrafiltration, the transmission of bovine serum albumin (BSA) and monoclonal antibody alemtuzumab (Campath-1H) through 300 kDa polyethersulfone (PES) ultrafiltration membranes were studied over a range of pH and salt concentrations, with focus on the likely conditions for achieving "reverse selectivity," i.e., obtaining purified alemtuzumab (approximately 155 kDa) in the permeate. Experimental results demonstrate that the reverse selectivity could be obtained by manipulating the operating conditions such as the solution pH, ionic strength, permeate flux, and system hydrodynamics. With a two-stage batch ultrafiltration process under suitable conditions, the monoclonal antibody alemtuzumab with a purity of > 98% was obtained in the permeate from a feed solution initially containing 0.50 g/l each of BSA and alemtuzumab. Further purity can be expected by selecting more suitable membranes and optimizing operating conditions.

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Section: Effects Of Stirring Speed and Permeate Fluxmentioning

confidence: 99%

Fractionation of bovine serum albumin and monoclonal antibody alemtuzumab using carrier phase ultrafiltration

Wang

Ghosh

Hale

et al. 2005

Biotech & Bioengineering

View full text Add to dashboard Cite

show abstract

“…If only the sizes of the pores are used as the means of separation with membranes, mostly 10-fold differences in molar masses of the proteins are needed because of the dispersed membrane pore sizes and fouling of the membranes. It is generally accepted that solutes whose molecular dimensions are small enough to permeate the membrane are substantially retained by the same membrane when larger solutes are present [5,6]. However, studies have shown that membrane filtration of proteins can also be drastically influenced by the nature of a solutesolute interaction [5][6][7][8].…”

Section: Introductionmentioning

confidence: 99%

“…It is generally accepted that solutes whose molecular dimensions are small enough to permeate the membrane are substantially retained by the same membrane when larger solutes are present [5,6]. However, studies have shown that membrane filtration of proteins can also be drastically influenced by the nature of a solutesolute interaction [5][6][7][8]. These physicochemical interactions can and do occur between the membrane and solutes in the form of electrostatic charge, hydrophobic or even charge transfer.…”

Section: Introductionmentioning

confidence: 99%

“…It is usually observed that proteins have the highest transmission at their isoelectric point (IEP) and lower transmissions when not at their IEP values [5,6,10,11]. For charged molecules such as proteinS, transport of rejected material back from the membrane surface to the bulk solution is not only dependent on the concentration gradient at the membrane interface but is also driven by the electrostatic repulsion between the charged molecules.…”

Section: Introductionmentioning

confidence: 99%

“…Noordman et al [5] have shown that rejection and fluxes of BSA retention can be well described by a model based on the MaxwellStefan theory of mass transfer with the nonidealities through the Carnahan-Starling equation of state for rigid spheres. The study was carried out by obtaining data for a single protein over a wide range of different environmental conditions, similar to those reported in literature elsewhere with respected to electrostatic interactions [7,9].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Membrane application in proteomic studies: Preliminary studies on the effect of pH, ionic strength and pressure on protein fractionation

Zulkali¹,

Ahmad²,

Chan³

2005

Desalination

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Intramodule pressure profiles and protein accumulation during tangential flow filtration

Cunha,

Zuponcic,

Rossi

et al. 2023

Biotechnology Progress

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Tangential flow filtration (TFF) through a 30 kDa nominal molecular weight cut‐off (MWCO) ultrafiltration membrane is widely employed to concentrate purified monoclonal antibodies (mAbs) to levels required for their formulation into injectable biologics. While TFF has been used to remove casein from milk for cheese production for over 35 years, and in pharmaceutical manufacture of biotherapeutic proteins for 20 years, the rapid decline in filtration rate (i.e., flux) at high protein concentrations is a limitation that still needs to be addressed. This is particularly important for mAbs, many of which are 140–160 kDa immunoglobulin G (IgG) type proteins recovered at concentrations of 200 mg/mL or higher. This work reports the direct measurement of local transmembrane pressure drops and off‐line confocal imaging of protein accumulation in stagnant regions on the surface of a 30 kDa regenerated cellulose membrane in a flat‐sheet configuration widely used in manufacture of biotherapeutic proteins. These first‐of‐a‐kind measurements using 150 kDa bovine IgG show that while axial pressure decreases by 58 psi across a process membrane cassette, the decrease in transmembrane pressure drop is constant at about 1.2 psi/cm along the 20.7 cm length of the membrane. Confocal laser scanning microscopy of the membrane surface at the completion of runs where retentate protein concentration exceeds 200 mg/mL, shows a 50 μm thick protein layer is uniformly deposited. The localized measurements made possible by the modified membrane system confirm the role of protein deposition on limiting ultrafiltration rate and indicate possible targets for improving membrane performance.

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Concentration and desalination of protein solutions by ultrafiltration

Cited by 38 publications

References 22 publications

Fractionation of bovine serum albumin and monoclonal antibody alemtuzumab using carrier phase ultrafiltration

Fractionation of bovine serum albumin and monoclonal antibody alemtuzumab using carrier phase ultrafiltration

Membrane application in proteomic studies: Preliminary studies on the effect of pH, ionic strength and pressure on protein fractionation

Intramodule pressure profiles and protein accumulation during tangential flow filtration

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