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Please use this identifier to cite or link to this item: http://eprint.iitd.ac.in/handle/2074/200

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dc.contributor.authorBalakrishnan, M-
dc.contributor.authorAgarwal, G P-
dc.date.accessioned2005-05-31T04:29:13Z-
dc.date.available2005-05-31T04:29:13Z-
dc.date.issued1996-
dc.identifier.citationJournal of Membrane Science 112 , 47-74en
dc.identifier.urihttp://eprint.iitd.ac.in/dspace/handle/2074/200-
dc.description.abstractProtein fractionation by ultrafiltration has elicited considerable interest in recent years. It is now recognised that a proper choice of the membrane and/or appropriate adjustment of operating conditions can successfully resolve binary protein mixtures. However, in order to identify the optimum conditions for selective filtration, it is essential to understand the UF characteristics of single proteins. In this paper, we have examined the flux and ransmission behavior of three different proteins, viz. lysozyme (13.93 kD, pl 10.6), ovalbumin (43.5 kD, pI 4.6) and myoglobin (16.89 kD, pI 6.8) as a function of operating variables in a vortex flow filter using 100 kD hydrophilic polyacrylonitrile membranes. The effects of both the module hydrodynamics, i.e. transmembrane pressure, axial velocity and rotation speed as well as the solution environment, i.e. protein concentration, ionic strength and pH were investigated. It was determined that ydrodynamics is primarily controlled by the transmembrane pressure and the membrane rotation rate. Also, variations in the feed solution properties, particularly the ionic strength and pH could dramatically alter the protein ransmission profiles. These results provide a basic framework for designing effective lysozyme/ovalbumin and lysozyme/myoglobin separations.en
dc.format.extent1,543,643 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoen-
dc.publisherElsevier Scienceen
dc.subjectUltrafiltrationen
dc.subjectVortex flow filteren
dc.subjectProtein transmissionen
dc.subjectModule hydrodynamicsen
dc.subjectSolution environmenten
dc.titleProtein fractionation in a vortex flow filter. I: Effect of systemhydrodynamics and solution environment on single protein transmissionen
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