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dc.contributor.authorIbáñez González, María José
dc.contributor.authorMazzuca Sobczuk, Tania
dc.contributor.authorRedondo Miranda, Rosa María
dc.contributor.authorMolina Grima, Emilio
dc.contributor.authorCooney, Charles
dc.date.accessioned2016-06-13T10:04:07Z
dc.date.available2016-06-13T10:04:07Z
dc.date.issued2016-07
dc.identifier.citationChemical Engineering Research and Design. Volume 111, July 2016, Pages 24–33es_ES
dc.identifier.urihttp://hdl.handle.net/10835/4334
dc.description.abstractThe purification of B-phycoerythrin from a concentrated extract of disrupted Porphyridium cruentum cells was carried out using a new vortex flow reactor design for protein purification. The reactor behaved as an expanded bed in the laminar vortices flow regime where the Streamline DEAE resin was expanded by the axial flow and stabilized by the vortex flow. After the broth culture was centrifuged and resuspended in the adsorption buffer, the concentrated extract of disrupted cells was directly loaded into the vortex flow reactor. The purification of B-phycoerythrin was carried out in two steps: adsorption in the expanded bed and elution from the settled bed. 142.0 mg of B-phycoerythrin was eluted representing a total recovery yield of 86.6%. Prior to B-phycoerythrin purification, the protein adsorption of the vortex flow reactor was characterized through hydrodynamic studies and a dynamic capacity measurement using a standard protein.es_ES
dc.language.isoenes_ES
dc.publisherElservieres_ES
dc.subjectProtein purificationes_ES
dc.subjectVortex flow reactores_ES
dc.titleA novel vortex flow reactor for the purification of B-phycoerythrin from Porphyridium cruentumes_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.relation.publisherversionhttp://authors.elsevier.com/a/1Sxtwx-vu8oDNes_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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