Characterization of ultrafiltration membranes by simultaneous streaming potential and flux measurements

Nyström, Marianne; Pihlajamäki, Arto; Ehsani, Neda

doi:10.1016/0376-7388(94)87031-4

Cited by 161 publications

(55 citation statements)

References 27 publications

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“…These observations were consistent with the isoelectric point of the modifier proteins. Membranes coated with protein foulant display isoelectric points slightly higher than the free protein (Nyström et al, 1994). The situation is similar here for membranes modified by covalent bonding of protein.…”

Section: Membrane Chargementioning

confidence: 56%

“…Before and after modification treatment, membrane compaction and initial water flux test were performed for 1 h at 100 kPa and 0.6 m s −1 crossflow using purified water (Millipore RO, <1 S cm −1 ). The crossflow cell was fitted with Ag/AgCl electrodes above and below the membrane for the purpose of measurement of streaming potential at a range of pressures <100 kPa using 10 −3 M KCl solution (Nyström et al, 1994). The streaming potential arises from the non-coincident distribution of fixed and mobile ions, and counter-ions during flow of solution through the pores of the membrane.…”

Section: Flow Cell For Flux and Streaming Potentialmentioning

confidence: 99%

“…Modification of the membrane in order to change its surface properties in terms of charge and hydrophobicity, has been investigated by many authors (Brink and Romijn, 1990;Ehsani and Nyström, 1995;Hvid et al, 1990;Kim et al, 1988;Kim and Fane, 1995;Nyström et al, 1989;Nyström and Järvinen, 1991;Nyström et al, 1994). Membranes have been modified by polymer coating, chemical adsorption or transformation, or exposure to high energy.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Modification of ultrafiltration membrane with gelatin protein

Stevens

Nyström

Ehsani

1998

Biotechnol. Bioeng.

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Section: Membrane Chargementioning

confidence: 56%

Section: Flow Cell For Flux and Streaming Potentialmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Modification of ultrafiltration membrane with gelatin protein

Stevens

Nyström

Ehsani

1998

Biotechnol. Bioeng.

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“…Surface deposition has been probed using techniques such as scanning electron microscopy (SEM) (Kim et al, 1992;Lee and Merson, 1975), AFM (Gesan et al, 1993;Makardij et al, 1999;Martinez et al, 2000), SEM coupled with Energy Dispersive X-ray (EDX) Spectroscopy (Rabiller-Baudry et al, 2002), UV microspectrophotometry (Reisterer et al, 1993), and confocal microscopy (Reichert et al, 2002). Pore and internal fouling by proteins has been examined by using standard infrared and x-ray photoelectron spectroscopy (XPS) (Labbe et al, 1990), radiolabeling (Robertson and Zydney, 1990), streaming potential measurements (Nystrom et al, 1994), transmission electron microscopy (TEM) (Kim et al, 1994;Sheldon et al, 1991), electron paramagnetic resonance spectroscopy (EPRS) (Oppenheim et al, 1994), attenuated total reflection Fourier-Transform Infra-Red Spectroscopy (ATR-FTIR) (Pihlajamaki et al, 1998) and small angle neutron scattering (SANS) (Su et al, 1998). Quantitative measurements have generally been undertaken by eluting proteins from fouled membranes followed by spectrophotometric determination or SDS-PAGE analysis of the total protein content (Fane et al, 1983;Suki et al, 1984;Tong et al, 1989).…”

Section: The Causes and Characterization Of Protein Fouling On Membranesmentioning

confidence: 99%

Quantitative analysis of membrane fouling by protein mixtures using MALDI‐MS

Chan¹,

Chen²,

Bucknall³

2003

Biotech & Bioengineering

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Binary aqueous solutions of bovine serum albumin (BSA) and beta-lactoglobulin (bLG) were subject to flux-stepping and constant flux ultrafiltration to identify the apparent critical flux and to study the mechanisms and factors affecting fouling when the membrane is permeable to one protein component. Membranes from these filtration experiments were analyzed using matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS) to locate and quantify levels of fouling below and above the apparent critical flux. Hydrophilic (PLTK) regenerated cellulose and hydrophobic (PBTK) polysulfone asymmetric membranes were used, both of 30 kDa nominal molecular weight cut-off. For the hydrophilic PLTK membrane, protein deposition was shown to depend on electrostatic forces, exhibiting little or no fouling when the proteins had the same charge sign as that of the membrane. This was found to apply for both dilute equal mass-per-unit-volume and equimolar binary mixtures. For the PBTK membrane, hydrophobic protein-membrane attractive forces were sufficiently strong to cause deposition of bLG even in the presence of repulsive electrostatic forces. For the PBTK membrane deposition exceeded monolayer coverage below and above apparent critical flux conditions but for the PLTK membrane this generally occurred when the apparent critical flux was exceeded. MALDI-MS was shown to be a facile direct analytical technique for individually quantifying adsorbed proteins on membrane surfaces at levels as low as 50 fmol/mm(2). The high levels of compound specificity inherent to mass spectrometry make this approach especially suited to the quantification of individual components in mixed deposits. In this study, MALDI-MS was found to be successful in identifying and quantifying the protein species responsible for fouling.

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“…One of the already available techniques measures streaming potential (SP) online through the pores of the membrane. From the streaming potential the zeta potential can be calculated [10][11][12]. The measurement can be done both during pure water flux experiments and during fouling or cleaning.…”

Section: Electrical Laser Magnetic and Acoustic Techniques In Membrmentioning

confidence: 99%