Thermodynamic studies of partitioning behavior of lysozyme and conalbumin in aqueous two-phase systems
Autor(a) principal: | |
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Data de Publicação: | 2009 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/1822/9569 |
Resumo: | The objective of this study was to determine the thermodynamic parameters (ΔtrG, ΔtrH and ΔtrS) associated with lysozyme and conalbumin partitioning in aqueous two-phases systems (ATPS). Influence of salt type and polyethylene glycol (PEG) concentrations on the partition coefficient of lysozyme and conalbumin from egg white was studied. The evaluated ATPS were composed of PEG 1500 and inorganic salts (sodium citrate and sodium sulfate) at a temperature of 25 °C and pH 7.0, with PEG 1500 g mol−1 concentrations of 14%, 16% and 18% (mass basis). Partitioning of lysozyme in PEG–citrate ATPS was enthalpically driven, however the PEG–sulfate ATPS was entropically driven. The tested systems can be employed for the separation of these two proteins in egg white, due to the fact that lysozyme migrates toward the polymeric phase and conalbumin to the saline phase in both ATPS. A high recovery of conalbumin in the saline phase of the PEG–sulfate ATPS was determined to be enthalpically driven. |
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Thermodynamic studies of partitioning behavior of lysozyme and conalbumin in aqueous two-phase systemsAqueous two-phase systemsEgg white proteinConalbuminLysozymeThermodynamic parametersScience & TechnologyThe objective of this study was to determine the thermodynamic parameters (ΔtrG, ΔtrH and ΔtrS) associated with lysozyme and conalbumin partitioning in aqueous two-phases systems (ATPS). Influence of salt type and polyethylene glycol (PEG) concentrations on the partition coefficient of lysozyme and conalbumin from egg white was studied. The evaluated ATPS were composed of PEG 1500 and inorganic salts (sodium citrate and sodium sulfate) at a temperature of 25 °C and pH 7.0, with PEG 1500 g mol−1 concentrations of 14%, 16% and 18% (mass basis). Partitioning of lysozyme in PEG–citrate ATPS was enthalpically driven, however the PEG–sulfate ATPS was entropically driven. The tested systems can be employed for the separation of these two proteins in egg white, due to the fact that lysozyme migrates toward the polymeric phase and conalbumin to the saline phase in both ATPS. A high recovery of conalbumin in the saline phase of the PEG–sulfate ATPS was determined to be enthalpically driven.National Council of Technological and Scientific Development (CNPq)Foundation to Research Support of the Minas Gerais State (FAPEMIG)Elsevier B.V.Universidade do MinhoSousa, Rita de Cássia Superbi deCoimbra, Jane Sélia dos ReisSilva, Luis Henrique Mendes daSilva, Maria do Carmo Hespanhol daRojas, Edwin Elard GarciaVicente, A. A.20092009-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/9569eng"Journal of Chromatography B". ISSN1570-0232. 877 (2009) 2579–2584.1570-023210.1016/j.jchromb.2009.07.00219617006info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-21T12:39:47Zoai:repositorium.sdum.uminho.pt:1822/9569Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:36:27.242534Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Thermodynamic studies of partitioning behavior of lysozyme and conalbumin in aqueous two-phase systems |
title |
Thermodynamic studies of partitioning behavior of lysozyme and conalbumin in aqueous two-phase systems |
spellingShingle |
Thermodynamic studies of partitioning behavior of lysozyme and conalbumin in aqueous two-phase systems Sousa, Rita de Cássia Superbi de Aqueous two-phase systems Egg white protein Conalbumin Lysozyme Thermodynamic parameters Science & Technology |
title_short |
Thermodynamic studies of partitioning behavior of lysozyme and conalbumin in aqueous two-phase systems |
title_full |
Thermodynamic studies of partitioning behavior of lysozyme and conalbumin in aqueous two-phase systems |
title_fullStr |
Thermodynamic studies of partitioning behavior of lysozyme and conalbumin in aqueous two-phase systems |
title_full_unstemmed |
Thermodynamic studies of partitioning behavior of lysozyme and conalbumin in aqueous two-phase systems |
title_sort |
Thermodynamic studies of partitioning behavior of lysozyme and conalbumin in aqueous two-phase systems |
author |
Sousa, Rita de Cássia Superbi de |
author_facet |
Sousa, Rita de Cássia Superbi de Coimbra, Jane Sélia dos Reis Silva, Luis Henrique Mendes da Silva, Maria do Carmo Hespanhol da Rojas, Edwin Elard Garcia Vicente, A. A. |
author_role |
author |
author2 |
Coimbra, Jane Sélia dos Reis Silva, Luis Henrique Mendes da Silva, Maria do Carmo Hespanhol da Rojas, Edwin Elard Garcia Vicente, A. A. |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Sousa, Rita de Cássia Superbi de Coimbra, Jane Sélia dos Reis Silva, Luis Henrique Mendes da Silva, Maria do Carmo Hespanhol da Rojas, Edwin Elard Garcia Vicente, A. A. |
dc.subject.por.fl_str_mv |
Aqueous two-phase systems Egg white protein Conalbumin Lysozyme Thermodynamic parameters Science & Technology |
topic |
Aqueous two-phase systems Egg white protein Conalbumin Lysozyme Thermodynamic parameters Science & Technology |
description |
The objective of this study was to determine the thermodynamic parameters (ΔtrG, ΔtrH and ΔtrS) associated with lysozyme and conalbumin partitioning in aqueous two-phases systems (ATPS). Influence of salt type and polyethylene glycol (PEG) concentrations on the partition coefficient of lysozyme and conalbumin from egg white was studied. The evaluated ATPS were composed of PEG 1500 and inorganic salts (sodium citrate and sodium sulfate) at a temperature of 25 °C and pH 7.0, with PEG 1500 g mol−1 concentrations of 14%, 16% and 18% (mass basis). Partitioning of lysozyme in PEG–citrate ATPS was enthalpically driven, however the PEG–sulfate ATPS was entropically driven. The tested systems can be employed for the separation of these two proteins in egg white, due to the fact that lysozyme migrates toward the polymeric phase and conalbumin to the saline phase in both ATPS. A high recovery of conalbumin in the saline phase of the PEG–sulfate ATPS was determined to be enthalpically driven. |
publishDate |
2009 |
dc.date.none.fl_str_mv |
2009 2009-01-01T00:00:00Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/1822/9569 |
url |
http://hdl.handle.net/1822/9569 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
"Journal of Chromatography B". ISSN1570-0232. 877 (2009) 2579–2584. 1570-0232 10.1016/j.jchromb.2009.07.002 19617006 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier B.V. |
publisher.none.fl_str_mv |
Elsevier B.V. |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799132894238605312 |