Application of the aqueous two-phase systems of ethylene and propylene oxide copolymer-maltodextrin for protein purification
- Autores
- Bolognese, Belén; Nerli, Bibiana Beatriz; Picó, Guillermo Alfredo
- Año de publicación
- 2005
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- In this study, the effect of several factors that govern the partitioning behaviour of three model proteins, such as bovine serum albumin, lysozyme and trypsin was analysed in a two-phase system formed by maltodextrin and a copolymer of ethylene and propylene oxides. The protein partition coefficient (K r) showed to be very sensitive to temperature changes, protein molecular weight, pH medium and the lyotropic ion presence. The phase diagram obtained for these novel polymer-polymer two-phase systems shows two phases with high polymer concentrations. The maltodextrin is enriched in the bottom phase while the copolymer of ethylene and propylene oxides is found in the upper phase. Since this copolymer is thermoreactive, the upper phase can be removed and heated above the copolymer's cloud point resulting in the formation of a new two-phase system with a lower water phase, containing the target protein and an upper copolymer-rich phase. Our results show that systems formed by maltodextrin and a copolymer of ethylene and propylene oxides may be considered as an interesting alternative to be used in protein purification due to their low cost, and also because they offer a viable solution to problems of polymer removal and recycling.
Fil: Bolognese, Belén. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina
Fil: Nerli, Bibiana Beatriz. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina
Fil: Picó, Guillermo Alfredo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina - Materia
-
ETHYLENE OXIDE PROPYLENE OXIDE RANDOM COPOLYMER
MALTODEXTRIN
PARTITIONING
TEMPERATURE-INDUCED TWO-PHASE SYSTEM - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/95223
Ver los metadatos del registro completo
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Application of the aqueous two-phase systems of ethylene and propylene oxide copolymer-maltodextrin for protein purificationBolognese, BelénNerli, Bibiana BeatrizPicó, Guillermo AlfredoETHYLENE OXIDE PROPYLENE OXIDE RANDOM COPOLYMERMALTODEXTRINPARTITIONINGTEMPERATURE-INDUCED TWO-PHASE SYSTEMhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1In this study, the effect of several factors that govern the partitioning behaviour of three model proteins, such as bovine serum albumin, lysozyme and trypsin was analysed in a two-phase system formed by maltodextrin and a copolymer of ethylene and propylene oxides. The protein partition coefficient (K r) showed to be very sensitive to temperature changes, protein molecular weight, pH medium and the lyotropic ion presence. The phase diagram obtained for these novel polymer-polymer two-phase systems shows two phases with high polymer concentrations. The maltodextrin is enriched in the bottom phase while the copolymer of ethylene and propylene oxides is found in the upper phase. Since this copolymer is thermoreactive, the upper phase can be removed and heated above the copolymer's cloud point resulting in the formation of a new two-phase system with a lower water phase, containing the target protein and an upper copolymer-rich phase. Our results show that systems formed by maltodextrin and a copolymer of ethylene and propylene oxides may be considered as an interesting alternative to be used in protein purification due to their low cost, and also because they offer a viable solution to problems of polymer removal and recycling.Fil: Bolognese, Belén. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; ArgentinaFil: Nerli, Bibiana Beatriz. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; ArgentinaFil: Picó, Guillermo Alfredo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; ArgentinaElsevier Science2005-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/95223Bolognese, Belén; Nerli, Bibiana Beatriz; Picó, Guillermo Alfredo; Application of the aqueous two-phase systems of ethylene and propylene oxide copolymer-maltodextrin for protein purification; Elsevier Science; Journal of Chromatography B; 814; 2; 1-2005; 347-3530378-43471570-0232CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1570023204008669info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jchromb.2004.10.057info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:09:46Zoai:ri.conicet.gov.ar:11336/95223instacron: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:34982025-09-03 10:09:47.262CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Application of the aqueous two-phase systems of ethylene and propylene oxide copolymer-maltodextrin for protein purification |
title |
Application of the aqueous two-phase systems of ethylene and propylene oxide copolymer-maltodextrin for protein purification |
spellingShingle |
Application of the aqueous two-phase systems of ethylene and propylene oxide copolymer-maltodextrin for protein purification Bolognese, Belén ETHYLENE OXIDE PROPYLENE OXIDE RANDOM COPOLYMER MALTODEXTRIN PARTITIONING TEMPERATURE-INDUCED TWO-PHASE SYSTEM |
title_short |
Application of the aqueous two-phase systems of ethylene and propylene oxide copolymer-maltodextrin for protein purification |
title_full |
Application of the aqueous two-phase systems of ethylene and propylene oxide copolymer-maltodextrin for protein purification |
title_fullStr |
Application of the aqueous two-phase systems of ethylene and propylene oxide copolymer-maltodextrin for protein purification |
title_full_unstemmed |
Application of the aqueous two-phase systems of ethylene and propylene oxide copolymer-maltodextrin for protein purification |
title_sort |
Application of the aqueous two-phase systems of ethylene and propylene oxide copolymer-maltodextrin for protein purification |
dc.creator.none.fl_str_mv |
Bolognese, Belén Nerli, Bibiana Beatriz Picó, Guillermo Alfredo |
author |
Bolognese, Belén |
author_facet |
Bolognese, Belén Nerli, Bibiana Beatriz Picó, Guillermo Alfredo |
author_role |
author |
author2 |
Nerli, Bibiana Beatriz Picó, Guillermo Alfredo |
author2_role |
author author |
dc.subject.none.fl_str_mv |
ETHYLENE OXIDE PROPYLENE OXIDE RANDOM COPOLYMER MALTODEXTRIN PARTITIONING TEMPERATURE-INDUCED TWO-PHASE SYSTEM |
topic |
ETHYLENE OXIDE PROPYLENE OXIDE RANDOM COPOLYMER MALTODEXTRIN PARTITIONING TEMPERATURE-INDUCED TWO-PHASE SYSTEM |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
In this study, the effect of several factors that govern the partitioning behaviour of three model proteins, such as bovine serum albumin, lysozyme and trypsin was analysed in a two-phase system formed by maltodextrin and a copolymer of ethylene and propylene oxides. The protein partition coefficient (K r) showed to be very sensitive to temperature changes, protein molecular weight, pH medium and the lyotropic ion presence. The phase diagram obtained for these novel polymer-polymer two-phase systems shows two phases with high polymer concentrations. The maltodextrin is enriched in the bottom phase while the copolymer of ethylene and propylene oxides is found in the upper phase. Since this copolymer is thermoreactive, the upper phase can be removed and heated above the copolymer's cloud point resulting in the formation of a new two-phase system with a lower water phase, containing the target protein and an upper copolymer-rich phase. Our results show that systems formed by maltodextrin and a copolymer of ethylene and propylene oxides may be considered as an interesting alternative to be used in protein purification due to their low cost, and also because they offer a viable solution to problems of polymer removal and recycling. Fil: Bolognese, Belén. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina Fil: Nerli, Bibiana Beatriz. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina Fil: Picó, Guillermo Alfredo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina |
description |
In this study, the effect of several factors that govern the partitioning behaviour of three model proteins, such as bovine serum albumin, lysozyme and trypsin was analysed in a two-phase system formed by maltodextrin and a copolymer of ethylene and propylene oxides. The protein partition coefficient (K r) showed to be very sensitive to temperature changes, protein molecular weight, pH medium and the lyotropic ion presence. The phase diagram obtained for these novel polymer-polymer two-phase systems shows two phases with high polymer concentrations. The maltodextrin is enriched in the bottom phase while the copolymer of ethylene and propylene oxides is found in the upper phase. Since this copolymer is thermoreactive, the upper phase can be removed and heated above the copolymer's cloud point resulting in the formation of a new two-phase system with a lower water phase, containing the target protein and an upper copolymer-rich phase. Our results show that systems formed by maltodextrin and a copolymer of ethylene and propylene oxides may be considered as an interesting alternative to be used in protein purification due to their low cost, and also because they offer a viable solution to problems of polymer removal and recycling. |
publishDate |
2005 |
dc.date.none.fl_str_mv |
2005-01 |
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/11336/95223 Bolognese, Belén; Nerli, Bibiana Beatriz; Picó, Guillermo Alfredo; Application of the aqueous two-phase systems of ethylene and propylene oxide copolymer-maltodextrin for protein purification; Elsevier Science; Journal of Chromatography B; 814; 2; 1-2005; 347-353 0378-4347 1570-0232 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/95223 |
identifier_str_mv |
Bolognese, Belén; Nerli, Bibiana Beatriz; Picó, Guillermo Alfredo; Application of the aqueous two-phase systems of ethylene and propylene oxide copolymer-maltodextrin for protein purification; Elsevier Science; Journal of Chromatography B; 814; 2; 1-2005; 347-353 0378-4347 1570-0232 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1570023204008669 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jchromb.2004.10.057 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/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 |
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1842270093914931200 |
score |
13.13397 |