Effect of Mg2+ binding on transmission of bovine serum albumin (BSA) through ultrafiltration membranes

Autores
Rodriguez Furlán, Laura Teresa; Campderrós, Mercedes E.
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Protein fractionation by membrane technology has many advantages for separations, in comparison with conventional methods. In this paper, the influence of different type and concentration of two electrolytes: NaCl and MgCl2 on buffer capacity and hydrodynamic radius of bovine plasma proteins were analyzed as a way to improve protein separation by cross-flow ultrafiltration. A tubular ceramic membrane with 0.2 m pore size was used. The evolution of permeate flux and BSA transmission was determined at 25○C and transmembrane pressure range of 0.2?1.4 bar. The membrane fouling was evaluated through the resistance model application, identifying the operational conditions of the highest BSA transmission through the membrane. In this regard, it was demonstrated that the effective radius of the protein and its buffering capacity were affected by the use of MgCl2 at 0.006 (w/v), which caused conformation changes in the protein structure resulting in a less resistance to transport.
Fil: Rodriguez Furlán, Laura Teresa. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto de Investigaciones en Tecnología Química; Argentina
Fil: Campderrós, Mercedes E.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto de Investigaciones En Tecnología Química; Argentina; Argentina. Universidad Nacional de San Luis; Argentina
Materia
Ultrafiltration
Bsa
Transmission
Protein Fractionation
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/14827
Acceder
id CONICETDig_2e199cdd9bb4ee380f922fba109fd359
oai_identifier_str oai:ri.conicet.gov.ar:11336/14827
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Effect of Mg2+ binding on transmission of bovine serum albumin (BSA) through ultrafiltration membranesRodriguez Furlán, Laura TeresaCampderrós, Mercedes E.UltrafiltrationBsaTransmissionProtein Fractionationhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Protein fractionation by membrane technology has many advantages for separations, in comparison with conventional methods. In this paper, the influence of different type and concentration of two electrolytes: NaCl and MgCl2 on buffer capacity and hydrodynamic radius of bovine plasma proteins were analyzed as a way to improve protein separation by cross-flow ultrafiltration. A tubular ceramic membrane with 0.2 m pore size was used. The evolution of permeate flux and BSA transmission was determined at 25○C and transmembrane pressure range of 0.2?1.4 bar. The membrane fouling was evaluated through the resistance model application, identifying the operational conditions of the highest BSA transmission through the membrane. In this regard, it was demonstrated that the effective radius of the protein and its buffering capacity were affected by the use of MgCl2 at 0.006 (w/v), which caused conformation changes in the protein structure resulting in a less resistance to transport.Fil: Rodriguez Furlán, Laura Teresa. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto de Investigaciones en Tecnología Química; ArgentinaFil: Campderrós, Mercedes E.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto de Investigaciones En Tecnología Química; Argentina; Argentina. Universidad Nacional de San Luis; ArgentinaElsevier Science2015-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/14827Rodriguez Furlán, Laura Teresa; Campderrós, Mercedes E.; Effect of Mg2+ binding on transmission of bovine serum albumin (BSA) through ultrafiltration membranes; Elsevier Science; Separation And Purification Technology; 150; 6-2015; 1-121383-5866enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1383586615300472info:eu-repo/semantics/altIdentifier/doi/10.1016/j.seppur.2015.06.021info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:37:34Zoai:ri.conicet.gov.ar:11336/14827instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:37:34.596CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Effect of Mg2+ binding on transmission of bovine serum albumin (BSA) through ultrafiltration membranes
title Effect of Mg2+ binding on transmission of bovine serum albumin (BSA) through ultrafiltration membranes
spellingShingle Effect of Mg2+ binding on transmission of bovine serum albumin (BSA) through ultrafiltration membranes
Rodriguez Furlán, Laura Teresa
Ultrafiltration
Bsa
Transmission
Protein Fractionation
title_short Effect of Mg2+ binding on transmission of bovine serum albumin (BSA) through ultrafiltration membranes
title_full Effect of Mg2+ binding on transmission of bovine serum albumin (BSA) through ultrafiltration membranes
title_fullStr Effect of Mg2+ binding on transmission of bovine serum albumin (BSA) through ultrafiltration membranes
title_full_unstemmed Effect of Mg2+ binding on transmission of bovine serum albumin (BSA) through ultrafiltration membranes
title_sort Effect of Mg2+ binding on transmission of bovine serum albumin (BSA) through ultrafiltration membranes
dc.creator.none.fl_str_mv Rodriguez Furlán, Laura Teresa
Campderrós, Mercedes E.
author Rodriguez Furlán, Laura Teresa
author_facet Rodriguez Furlán, Laura Teresa
Campderrós, Mercedes E.
author_role author
author2 Campderrós, Mercedes E.
author2_role author
dc.subject.none.fl_str_mv Ultrafiltration
Bsa
Transmission
Protein Fractionation
topic Ultrafiltration
Bsa
Transmission
Protein Fractionation
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Protein fractionation by membrane technology has many advantages for separations, in comparison with conventional methods. In this paper, the influence of different type and concentration of two electrolytes: NaCl and MgCl2 on buffer capacity and hydrodynamic radius of bovine plasma proteins were analyzed as a way to improve protein separation by cross-flow ultrafiltration. A tubular ceramic membrane with 0.2 m pore size was used. The evolution of permeate flux and BSA transmission was determined at 25○C and transmembrane pressure range of 0.2?1.4 bar. The membrane fouling was evaluated through the resistance model application, identifying the operational conditions of the highest BSA transmission through the membrane. In this regard, it was demonstrated that the effective radius of the protein and its buffering capacity were affected by the use of MgCl2 at 0.006 (w/v), which caused conformation changes in the protein structure resulting in a less resistance to transport.
Fil: Rodriguez Furlán, Laura Teresa. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto de Investigaciones en Tecnología Química; Argentina
Fil: Campderrós, Mercedes E.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto de Investigaciones En Tecnología Química; Argentina; Argentina. Universidad Nacional de San Luis; Argentina
description Protein fractionation by membrane technology has many advantages for separations, in comparison with conventional methods. In this paper, the influence of different type and concentration of two electrolytes: NaCl and MgCl2 on buffer capacity and hydrodynamic radius of bovine plasma proteins were analyzed as a way to improve protein separation by cross-flow ultrafiltration. A tubular ceramic membrane with 0.2 m pore size was used. The evolution of permeate flux and BSA transmission was determined at 25○C and transmembrane pressure range of 0.2?1.4 bar. The membrane fouling was evaluated through the resistance model application, identifying the operational conditions of the highest BSA transmission through the membrane. In this regard, it was demonstrated that the effective radius of the protein and its buffering capacity were affected by the use of MgCl2 at 0.006 (w/v), which caused conformation changes in the protein structure resulting in a less resistance to transport.
publishDate 2015
dc.date.none.fl_str_mv 2015-06
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/14827
Rodriguez Furlán, Laura Teresa; Campderrós, Mercedes E.; Effect of Mg2+ binding on transmission of bovine serum albumin (BSA) through ultrafiltration membranes; Elsevier Science; Separation And Purification Technology; 150; 6-2015; 1-12
1383-5866
url http://hdl.handle.net/11336/14827
identifier_str_mv Rodriguez Furlán, Laura Teresa; Campderrós, Mercedes E.; Effect of Mg2+ binding on transmission of bovine serum albumin (BSA) through ultrafiltration membranes; Elsevier Science; Separation And Purification Technology; 150; 6-2015; 1-12
1383-5866
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1383586615300472
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.seppur.2015.06.021
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1844613183629688832
score 13.070432

Publicaciones similares