Hydrophobic interaction adsorption of whey proteins: effect of temperature and salt concentration and thermodynamic analysis
Autor(a) principal: | |
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Data de Publicação: | 2006 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | LOCUS Repositório Institucional da UFV |
Texto Completo: | https://doi.org/10.1016/j.jchromb.2006.06.021 http://www.locus.ufv.br/handle/123456789/22401 |
Resumo: | The adsorptive behavior of bovine serum albumin (BSA) and β-lactoglobulin (β-lg) on hydrophobic adsorbent was studied at four temperatures and different salt concentrations. The Langmuir model was fitted by experimental equilibrium data showing that an increase in temperature and salt concentration results in an increase on the capacity factor of both proteins. A thermodynamic analysis coupled with isotherm measurements showed that salt concentration and temperature affected the enthalpic and entropic behavior of the adsorption process of both proteins, mainly to the β-lg. The fast variation in the Z value for temperature over than 303.1 K suggest a great conformational change occurring in the β-lg structure, which almost duplicated the maximum adsorption capacity of this protein. |
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Minim, Luis A.Bonomo, Renata C. F.Coimbra, Jane S. R.Fontan, Rafael C. I.Silva, Luis H. Mendes daMinim, Valéria P. R.2018-10-25T11:14:52Z2018-10-25T11:14:52Z2006-11-2115700232https://doi.org/10.1016/j.jchromb.2006.06.021http://www.locus.ufv.br/handle/123456789/22401The adsorptive behavior of bovine serum albumin (BSA) and β-lactoglobulin (β-lg) on hydrophobic adsorbent was studied at four temperatures and different salt concentrations. The Langmuir model was fitted by experimental equilibrium data showing that an increase in temperature and salt concentration results in an increase on the capacity factor of both proteins. A thermodynamic analysis coupled with isotherm measurements showed that salt concentration and temperature affected the enthalpic and entropic behavior of the adsorption process of both proteins, mainly to the β-lg. The fast variation in the Z value for temperature over than 303.1 K suggest a great conformational change occurring in the β-lg structure, which almost duplicated the maximum adsorption capacity of this protein.engJournal of Chromatography Bv. 844, n. 1, p. 6- 14, nov. 2006Elsevier B.V.info:eu-repo/semantics/openAccessBovine serum albuminβ- LactoglobulinThermodynamic parametersIsothermHydrophobic interactionHydrophobic interaction adsorption of whey proteins: effect of temperature and salt concentration and thermodynamic analysisinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINALartigo.pdfartigo.pdftexto completoapplication/pdf526424https://locus.ufv.br//bitstream/123456789/22401/1/artigo.pdf40f37360e771d2584110598ec7d925f6MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/22401/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52123456789/224012018-10-25 08:15:18.963oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452018-10-25T11:15:18LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false |
dc.title.en.fl_str_mv |
Hydrophobic interaction adsorption of whey proteins: effect of temperature and salt concentration and thermodynamic analysis |
title |
Hydrophobic interaction adsorption of whey proteins: effect of temperature and salt concentration and thermodynamic analysis |
spellingShingle |
Hydrophobic interaction adsorption of whey proteins: effect of temperature and salt concentration and thermodynamic analysis Minim, Luis A. Bovine serum albumin β- Lactoglobulin Thermodynamic parameters Isotherm Hydrophobic interaction |
title_short |
Hydrophobic interaction adsorption of whey proteins: effect of temperature and salt concentration and thermodynamic analysis |
title_full |
Hydrophobic interaction adsorption of whey proteins: effect of temperature and salt concentration and thermodynamic analysis |
title_fullStr |
Hydrophobic interaction adsorption of whey proteins: effect of temperature and salt concentration and thermodynamic analysis |
title_full_unstemmed |
Hydrophobic interaction adsorption of whey proteins: effect of temperature and salt concentration and thermodynamic analysis |
title_sort |
Hydrophobic interaction adsorption of whey proteins: effect of temperature and salt concentration and thermodynamic analysis |
author |
Minim, Luis A. |
author_facet |
Minim, Luis A. Bonomo, Renata C. F. Coimbra, Jane S. R. Fontan, Rafael C. I. Silva, Luis H. Mendes da Minim, Valéria P. R. |
author_role |
author |
author2 |
Bonomo, Renata C. F. Coimbra, Jane S. R. Fontan, Rafael C. I. Silva, Luis H. Mendes da Minim, Valéria P. R. |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Minim, Luis A. Bonomo, Renata C. F. Coimbra, Jane S. R. Fontan, Rafael C. I. Silva, Luis H. Mendes da Minim, Valéria P. R. |
dc.subject.pt-BR.fl_str_mv |
Bovine serum albumin β- Lactoglobulin Thermodynamic parameters Isotherm Hydrophobic interaction |
topic |
Bovine serum albumin β- Lactoglobulin Thermodynamic parameters Isotherm Hydrophobic interaction |
description |
The adsorptive behavior of bovine serum albumin (BSA) and β-lactoglobulin (β-lg) on hydrophobic adsorbent was studied at four temperatures and different salt concentrations. The Langmuir model was fitted by experimental equilibrium data showing that an increase in temperature and salt concentration results in an increase on the capacity factor of both proteins. A thermodynamic analysis coupled with isotherm measurements showed that salt concentration and temperature affected the enthalpic and entropic behavior of the adsorption process of both proteins, mainly to the β-lg. The fast variation in the Z value for temperature over than 303.1 K suggest a great conformational change occurring in the β-lg structure, which almost duplicated the maximum adsorption capacity of this protein. |
publishDate |
2006 |
dc.date.issued.fl_str_mv |
2006-11-21 |
dc.date.accessioned.fl_str_mv |
2018-10-25T11:14:52Z |
dc.date.available.fl_str_mv |
2018-10-25T11:14:52Z |
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 |
https://doi.org/10.1016/j.jchromb.2006.06.021 http://www.locus.ufv.br/handle/123456789/22401 |
dc.identifier.issn.none.fl_str_mv |
15700232 |
identifier_str_mv |
15700232 |
url |
https://doi.org/10.1016/j.jchromb.2006.06.021 http://www.locus.ufv.br/handle/123456789/22401 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartofseries.pt-BR.fl_str_mv |
v. 844, n. 1, p. 6- 14, nov. 2006 |
dc.rights.driver.fl_str_mv |
Elsevier B.V. info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
Elsevier B.V. |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Journal of Chromatography B |
publisher.none.fl_str_mv |
Journal of Chromatography B |
dc.source.none.fl_str_mv |
reponame:LOCUS Repositório Institucional da UFV instname:Universidade Federal de Viçosa (UFV) instacron:UFV |
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Universidade Federal de Viçosa (UFV) |
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UFV |
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LOCUS Repositório Institucional da UFV |
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LOCUS Repositório Institucional da UFV |
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LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV) |
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