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Article: The role of hydrodynamic conditions and solution chemistry on protein fouling during ultrafiltration

TitleThe role of hydrodynamic conditions and solution chemistry on protein fouling during ultrafiltration
Authors
KeywordsBovine Serum Albumin (Bsa)
Hydrodynamic Conditions
Ionic Strength
Membrane Fouling
Protein
Ultrafiltration
Issue Date2009
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/desal
Citation
Desalination, 2009, v. 249 n. 3, p. 1079-1087 How to Cite?
AbstractThis study investigates the effect of hydrodynamic conditions and solution chemistry on protein fouling during ultrafiltration. Drastic flux reduction was observed at high initial flux and/or low cross-flow velocity. A limiting flux existed during BSA filtration, beyond which membrane flux cannot be sustained. Further increase in pressure over the limiting value did not enhance the stable flux. The rate and extent of BSA fouling were also strongly dependent on the feedwater composition, such as BSA concentration, pH, and ionic strength. Foulant concentration had no effect on the stable flux, although the rate approaching to the stable flux increased proportionally with increasing foulant concentration. Fouling was most severe at the isoelectric point of BSA (pH 4.7), where the electrostatic repulsion between foulant molecules is negligible. Membrane fouling became less severe at pHs away from the isoelectric point. Increasing ionic strength at pH 3.0 promoted severe fouling likely due to electric double layer (EDL) compression. On the other hand, the flux behavior was insensitive to salt concentration at pH 4.7 due to the lack of electrostatic interaction. At a solution pH of 5.8, effect of ionic strength on long-term flux behavior was directly opposite to that on the transient behavior. While the long-term flux was lower at higher ionic strength due to EDL compression, the transient behavior was also affected by the BSA retention of the membrane. © 2009 Elsevier B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/185386
ISSN
2015 Impact Factor: 4.412
2015 SCImago Journal Rankings: 1.549
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorShe, Qen_US
dc.contributor.authorTang, CYen_US
dc.contributor.authorWang, YNen_US
dc.contributor.authorZhang, Zen_US
dc.date.accessioned2013-07-30T07:32:06Z-
dc.date.available2013-07-30T07:32:06Z-
dc.date.issued2009en_US
dc.identifier.citationDesalination, 2009, v. 249 n. 3, p. 1079-1087en_US
dc.identifier.issn0011-9164en_US
dc.identifier.urihttp://hdl.handle.net/10722/185386-
dc.description.abstractThis study investigates the effect of hydrodynamic conditions and solution chemistry on protein fouling during ultrafiltration. Drastic flux reduction was observed at high initial flux and/or low cross-flow velocity. A limiting flux existed during BSA filtration, beyond which membrane flux cannot be sustained. Further increase in pressure over the limiting value did not enhance the stable flux. The rate and extent of BSA fouling were also strongly dependent on the feedwater composition, such as BSA concentration, pH, and ionic strength. Foulant concentration had no effect on the stable flux, although the rate approaching to the stable flux increased proportionally with increasing foulant concentration. Fouling was most severe at the isoelectric point of BSA (pH 4.7), where the electrostatic repulsion between foulant molecules is negligible. Membrane fouling became less severe at pHs away from the isoelectric point. Increasing ionic strength at pH 3.0 promoted severe fouling likely due to electric double layer (EDL) compression. On the other hand, the flux behavior was insensitive to salt concentration at pH 4.7 due to the lack of electrostatic interaction. At a solution pH of 5.8, effect of ionic strength on long-term flux behavior was directly opposite to that on the transient behavior. While the long-term flux was lower at higher ionic strength due to EDL compression, the transient behavior was also affected by the BSA retention of the membrane. © 2009 Elsevier B.V. All rights reserved.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/desalen_US
dc.relation.ispartofDesalinationen_US
dc.subjectBovine Serum Albumin (Bsa)en_US
dc.subjectHydrodynamic Conditionsen_US
dc.subjectIonic Strengthen_US
dc.subjectMembrane Foulingen_US
dc.subjectProteinen_US
dc.subjectUltrafiltrationen_US
dc.titleThe role of hydrodynamic conditions and solution chemistry on protein fouling during ultrafiltrationen_US
dc.typeArticleen_US
dc.identifier.emailTang, CY: tangc@hku.hken_US
dc.identifier.authorityTang, CY=rp01765en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.desal.2009.05.015en_US
dc.identifier.scopuseid_2-s2.0-71649111646en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-71649111646&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume249en_US
dc.identifier.issue3en_US
dc.identifier.spage1079en_US
dc.identifier.epage1087en_US
dc.identifier.isiWOS:000272438500027-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridShe, Q=34868602200en_US
dc.identifier.scopusauthoridTang, CY=35489259800en_US
dc.identifier.scopusauthoridWang, YN=35076853300en_US
dc.identifier.scopusauthoridZhang, Z=8369756300en_US

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