2000
DOI: 10.1006/jcis.1999.6575
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Protein Adsorption and Deposition onto Microfiltration Membranes: The Role of Solute–Solid Interactions

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Cited by 44 publications
(29 citation statements)
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“…UF of PPW at pH 6.74 hence is desirable because it avoids protein coagulation or agglomeration that could result in severe adverse effects on membrane performance (Lo et al, 2005). Similar observations were reported with low concentration γ-globulin and the membrane surfaces were found relevant for the first layer of protein adsorption (Martinez et al, 2000).…”
Section: Flux Behavior During Ultrafiltrationmentioning
confidence: 69%
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“…UF of PPW at pH 6.74 hence is desirable because it avoids protein coagulation or agglomeration that could result in severe adverse effects on membrane performance (Lo et al, 2005). Similar observations were reported with low concentration γ-globulin and the membrane surfaces were found relevant for the first layer of protein adsorption (Martinez et al, 2000).…”
Section: Flux Behavior During Ultrafiltrationmentioning
confidence: 69%
“…Further, when the wastewater was acidified with hydrochloric acid from its regular pH 6.6 to pH 3.0, it became less colloidal and, at this low pH, the membrane flux significantly increased to 490-570 L m − 2 day − 1 , compared to 330-390 L m − 2 day − 1 at pH 6.6 (Shih & Kozink, 1980). It is well recognized that the pH value of a solution is highly influential on the conformation of protein molecules, as the electrical properties of protein molecules play an important role in determining their interactions with the membrane surface (Martinez et al, 2000). Therefore to assess the effect of pH on the UF flux, the isoelectric point (pI) of the protein recovered from PPW was determined.…”
Section: Flux Behavior During Ultrafiltrationmentioning
confidence: 94%
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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).…”
Section: The Causes and Characterization Of Protein Fouling On Membranesmentioning
confidence: 99%
“…All these models assume the same energy adsorption sites on the surface of the adsorbent, the linear form is expressed by the equation [6] .…”
Section: Langmuir Modelmentioning
confidence: 99%