Effect of Mg2+ binding on transmission of bovine serum albumin (BSA) through ultrafiltration membranes (original) (raw)

Role of electrophoretic mobility of protein on its retention by an ultrafiltration membrane

Journal of Chromatography B: Biomedical Sciences and Applications, 2001

Lysozyme and lactoferrin, two globular proteins, were first studied separately in order to elaborate a strategy for the improvement of their separation by ultrafiltration (UF) with zirconia-based membranes of different charge sign and pore radius. The electrophoretic mobility (m) at fixed pH and variable ionic strength was used for the characterisation of both proteins and zirconia particles, similar to the active layer of the membrane during the UF run. Specific adsorption of phosphate ions was shown for both proteins resulting in new isoelectric points. The occurrence of electrostatic exclusion mechanism in addition to the molecular sieving in UF of charged solutes was shown for: • Low molecular weight solute: multivalent citrate at pH 6 was specifically adsorbed on zirconia and its transmission through the membrane (defined as the ratio of the concentration in the permeate to that of the feed solution) was reduced 21 in the range 0.001-0.01 mol l of citrate concentration • Proteins: their transmissions increase when the ionic strength increases (ion-exchange is not the relevant mechanism because transmission is irrespective of the initial charge of the membrane compared with the protein charge). A model based on convection, diffusion and electrophoretic migration mechanisms (CDE model) was proposed to take into account this behaviour. The CDE model predicts the possible existence of a depleted sub-layer of the charged protein in the concentration polarisation layer, located in the close vicinity of the membrane surface. A strategy for the separation of two proteins in mixed solution was proposed by varying both the physico-chemical environment in the feed solution (pH, ionic strength, chemical nature of the electrolyte) and the membrane pore radius. Maximum selectivity was obtained when the target protein (to be transmitted in the permeate side) is close to being uncharged due to specific adsorption of electrolyte ions. Ultrafiltration selectivity is enhanced with membrane of large pore radius, which provides high transmission of the target protein and efficient electrostatic exclusion of the solute to be retained in the retentate side. This UF approach corresponds roughly to the separation of one uncharged and one charged protein from a mixed solution by size exclusion chromatography of the uncharged protein combined with electrostatic exclusion of the charged protein due to packing of similar charge.

The performance of bovine serum albumin filtration by using polyethersulfone-Tetronic 304 blend Ultrafiltration Membrane

F1000Research

Background: Membrane technology has been widely applied for protein purification. In applications for protein separation, a membrane with stable filtration performance is necessary. In this work, two types of hollow fiber membranes with different characteristic were used to study the filtration profile of bovine serum albumin. Methods: A single piece of hollow fiber module was used for ultrafiltration testing using UF0 and UFT304 membranes. Flux and rejection of BSA solution were collected based on a pressure-driven inside filtration model. Results: Ultrafiltration experiments showed that the flux of UFT304 membrane was higher than that of UF0 membrane in all applied pressure condition. Solute rejection was achieved up to 90% for ultrafiltration of BSA solution by using UF0 membrane obtained on the operating pressure of 0.5 atm. Conclusion: In general, UFT304 membranes has better ultrafiltration performance for BSA separation than UF0 membranes. The UFT304 membrane has a more stable...

Analysis of Protein Separation Mechanism in Charged Ultrafiltration Membrane

Journal of Engineering and Technological Sciences, 2018

The separation mechanism of proteins on a charged ultrafiltration membrane was analyzed using the extended Nernst-Planck (N-P) model. The model was solved numerically based on experimental data during ultrafiltration of bovine serum albumin/BSA and hemoglobin at various pH (between 5 and 8) to obtain the flux parameter (J v). The flux parameter was used to determine the effective charge of the membrane () and the actual membrane porosity (A k). These two parameters were then used to predict the transport mechanism of proteins through the charged membrane. Higher flux was obtained during the ultrafiltration of BSA compared to hemoglobin. The most effective separation of mixed proteins occurred at pH 5 ( albumin = 5). In addition, the mobility of a single protein was lower than when it was mixed with other proteins that had different charges. The effective charges of the membranes were varied between 0.99996 to 1.0000, which means that the fixed charge on the membrane structure was higher than the concentration of proteins, thus the effective charge of the membrane was not influenced by the presence of protein charge at various pH. On the contrary, the value of A k was influenced by the type and charge of the proteins. A decrease of negative charge along with an increase of solution pH increased the porosity of the membrane, thus reducing the rejection of proteins.

The Clogging Effect in the Process of Protein Separation by Ultrafiltration

Materiale Plastice, 2020

In this study, five ultrafiltration membranes (polysulfone, cellulose acetate and polyethersulfone) were tested in the treatment of aqueous protein solutions similar to wastewater from fermentation industries. The experiments were made in tangential flow filtration. The permeate flux for the five membranes tested at the optimum pressure of 3 bar decreased due to the effect of clogging the pores by the macromolecular protein solutions. Cellulose acetate membranes showed the lowest permeate flux (Ac-Cel1=152.4 L/m 2 .h and Ac-Cel2=40.3 L/m 2 .h) which doesn't recommend them for the ultrafiltration process of bovine serum albumin. When a polysulfone membrane was used in several cycles of protein-containing wastewater ultrafiltration, the permeate flow decreased progressively from one cycle to another due to the internal clogging of the membrane (501.6 L/m 2 .h up to 444.0 L/m 2 .h). Regarding the ultrafiltration of protein solutions with a suspended yeast content, the clogging was predominant on the membrane's surface, which results in a decrease of the permeate flux by over 50%.

Effects of Ionic Environments on Bovine Serum Albumin Fouling in a Cross-Flow Ultrafiltration System

Chemical Engineering & Technology, 2007

The influence of electrostatic interactions on membrane fouling during the separation of bovine serum albumin (BSA) from solution was studied in a crossflow ultrafiltration system. Experiments were carried out at different pH values between 3.78 and 7.46; and for different ionic strengths between 0.001 M and 0.1 M. The changes in permeate flux, cake layer resistance, zeta potentials of BSA and polyether sulfone (PES) membranes, and electrostatic interaction energies, were evaluated. At all of the ionic conditions studied, PES membranes are negatively charged. However, BSA molecules are either negatively or positively charged depending on the ionic environment. Whereas the cake layer resistance decreased with increasing pH and ionic strength, the permeate fluxes increased. The calculated electrostatic energy was a minimum at the isoelectric point (IEP) of BSA. However, at this point, the cake resistances corresponding to fouling at each ionic strength, were not minimized. Below the IEP of BSA, the electrostatic forces were attractive, while above the IEP, repulsive electrostatic forces were dominant.

Preparation and characterization of a polysulfone ultrafiltration membrane for bovine serum albumin separation: Effect of polymer concentration

Desalination and Water Treatment, 2011

This study aimed to investigate the effect of polymer concentration on the morphology and performance of an asymmetric ultrafiltration (UF) membrane for bovine serum albumin (BSA) separation. Flat sheet asymmetric UF membranes were fabricated via dry/wet phase inversion technique. These fabricated membranes were characterized in terms of membrane morphology, membrane pore radius and membrane surface charge. The membrane performance was determined based on pure water flux, sodium chloride rejection and BSA permeation test. Promising results were obtained when BSA rejection ranged from 94.3% to 100%. The optimum membrane in this study was determined by PSF 17% (containing 17 wt% polymer concentration) which successfully exhibited 100% rejection with filtrate flux for about 23.86 L/m2.h at a pressure of 2 bar. This research also proved that polymer concentration would greatly affect the membrane performance and structural properties, consecutively enhancing the membranes ability for BSA separation.

Effects of Solution Properties on Solute and Permeate Flux in Bovine Serum Albumin-IgG Ultrafiltration

Biotechnology Progress, 1994

It has been observed that bovine serum albumin (BSA, 69 000 Da) exhibits high rejection in a pH 7.4,0.15 M NaCl solution containing low concentrations of immunoy-globulins (16,155 000 Da). Although it is apparent that this phenomenon is likely due to the complex interactions of the proteins as well as to simple steric hindrance, it is not clear to what extent these resistances contribute to the solute flux loss. This study investigates how variations in IgG concentration, solution pH, and ionic strength can affect the solute and the permeate fluxes for the ultrafiltration of BSA through 100 000 MWCO cellulosic membranes in a batch cell. The results showed that, unlike cases performed at pH 7.4 in 0.15 M NaC1, the presence of IgG may increase the transport of BSA under certain conditions. This study does show the potential value and insights that will result from further binary protein ultrafiltration research.

Albumin denaturation during ultrafiltration: Effects of operating conditions and consequences on membrane fouling

Biotechnology and Bioengineering, 1991

Ultrafiltration of high-purity grade bovine serum albumin has been carried out under various temperature between 5 and 30°C and at various cross-flow velocities, pressures, and concentrations with the aim of studying protein denaturation and its consequences on the process. Three different pump heads have been tested. Denaturation of proteins in solution has been monitored by laser light scattering and size exclusion chromatography. The rate of protein denaturation increases with temperature, cross-flow, and time. It is observed that membrane fouling is different whether denaturation has occurred or not. Under high-concentration polarization, denaturation can occur in the boundary layer if the wall concentration exceeds 400 g/L. It is shown how the residence time, operating temperature, and pressure play an important part in membrane fouling. This can provide guidelines for process design and control.

The effect of protein–protein and protein–membrane interactions on membrane fouling in ultrafiltration

Journal of Membrane Science, 2000

It was studied how protein-protein and protein-membrane interactions influence the filtration performance during the ultrafiltration of protein solutions over polymeric membranes. This was done by measuring flux, streaming potential, and protein transmission during filtration of bovine serum albumin (BSA) solutions at various pH values using various membranes with different cut-off values.