Selective coacervation between lactoferrin and the two isoforms of β-lactoglobulin

Detalhes bibliográficos
Autor(a) principal: Tavares, Guilherme M.
Data de Publicação: 2015
Outros Autores: Croguennec, Thomas, Hamon, Pascaline, Carvalho, Antônio F., Bouhallab, Saïd
Tipo de documento: Artigo
Idioma: eng
Título da fonte: LOCUS Repositório Institucional da UFV
Texto Completo: https://doi.org/10.1016/j.foodhyd.2015.02.027
http://www.locus.ufv.br/handle/123456789/22644
Resumo: This work reports on the impact of subtle change of protein charge on coacervation and subsequent liquid–liquid phase separation between two oppositely charged globular proteins. For this purpose, a comparative study was conducted on the coacervation of lactoferrin (LF) with the two β-lactoglobulin (β-LG) isoforms. Upon mixing LF with an excess of β-LG, microspheres were formed throughout coacervation under narrow pH range (5.4–6.0). At the optimal pH of coacervation, LF being the limiting partner under tested concentration ranges. The β-LG/LF molar ratio recovered in the formed coacervates varied from 4 to 8 depending on the total protein concentration. Remarkably, LF showed a selective coacervation with isoform A of β-LG as judged by a larger concentration domain for coacervation and a high yield of LF recovered once mixed with β-LG A i.e. 80% against a maximum of 42% with β-LG B. At thermodynamic level, the interaction of LF with both β-LG isoforms exhibited complex exothermic binding isotherms with both enthalpic and entropic contributions.
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spelling Selective coacervation between lactoferrin and the two isoforms of β-lactoglobulinβ-Lactoglobulin isoformsLactoferrinCo-assemblyMicrospheresCoacervatesThis work reports on the impact of subtle change of protein charge on coacervation and subsequent liquid–liquid phase separation between two oppositely charged globular proteins. For this purpose, a comparative study was conducted on the coacervation of lactoferrin (LF) with the two β-lactoglobulin (β-LG) isoforms. Upon mixing LF with an excess of β-LG, microspheres were formed throughout coacervation under narrow pH range (5.4–6.0). At the optimal pH of coacervation, LF being the limiting partner under tested concentration ranges. The β-LG/LF molar ratio recovered in the formed coacervates varied from 4 to 8 depending on the total protein concentration. Remarkably, LF showed a selective coacervation with isoform A of β-LG as judged by a larger concentration domain for coacervation and a high yield of LF recovered once mixed with β-LG A i.e. 80% against a maximum of 42% with β-LG B. At thermodynamic level, the interaction of LF with both β-LG isoforms exhibited complex exothermic binding isotherms with both enthalpic and entropic contributions.Food Hydrocolloids2018-11-29T13:12:44Z2018-11-29T13:12:44Z2015-06info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlepdfapplication/pdf0268005Xhttps://doi.org/10.1016/j.foodhyd.2015.02.027http://www.locus.ufv.br/handle/123456789/22644engVolume 48, Pages 238- 247, June 20152015 Elsevier Ltd. All rights reservedinfo:eu-repo/semantics/openAccessTavares, Guilherme M.Croguennec, ThomasHamon, PascalineCarvalho, Antônio F.Bouhallab, Saïdreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFV2024-07-12T06:29:29Zoai:locus.ufv.br:123456789/22644Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452024-07-12T06:29:29LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false
dc.title.none.fl_str_mv Selective coacervation between lactoferrin and the two isoforms of β-lactoglobulin
title Selective coacervation between lactoferrin and the two isoforms of β-lactoglobulin
spellingShingle Selective coacervation between lactoferrin and the two isoforms of β-lactoglobulin
Tavares, Guilherme M.
β-Lactoglobulin isoforms
Lactoferrin
Co-assembly
Microspheres
Coacervates
title_short Selective coacervation between lactoferrin and the two isoforms of β-lactoglobulin
title_full Selective coacervation between lactoferrin and the two isoforms of β-lactoglobulin
title_fullStr Selective coacervation between lactoferrin and the two isoforms of β-lactoglobulin
title_full_unstemmed Selective coacervation between lactoferrin and the two isoforms of β-lactoglobulin
title_sort Selective coacervation between lactoferrin and the two isoforms of β-lactoglobulin
author Tavares, Guilherme M.
author_facet Tavares, Guilherme M.
Croguennec, Thomas
Hamon, Pascaline
Carvalho, Antônio F.
Bouhallab, Saïd
author_role author
author2 Croguennec, Thomas
Hamon, Pascaline
Carvalho, Antônio F.
Bouhallab, Saïd
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Tavares, Guilherme M.
Croguennec, Thomas
Hamon, Pascaline
Carvalho, Antônio F.
Bouhallab, Saïd
dc.subject.por.fl_str_mv β-Lactoglobulin isoforms
Lactoferrin
Co-assembly
Microspheres
Coacervates
topic β-Lactoglobulin isoforms
Lactoferrin
Co-assembly
Microspheres
Coacervates
description This work reports on the impact of subtle change of protein charge on coacervation and subsequent liquid–liquid phase separation between two oppositely charged globular proteins. For this purpose, a comparative study was conducted on the coacervation of lactoferrin (LF) with the two β-lactoglobulin (β-LG) isoforms. Upon mixing LF with an excess of β-LG, microspheres were formed throughout coacervation under narrow pH range (5.4–6.0). At the optimal pH of coacervation, LF being the limiting partner under tested concentration ranges. The β-LG/LF molar ratio recovered in the formed coacervates varied from 4 to 8 depending on the total protein concentration. Remarkably, LF showed a selective coacervation with isoform A of β-LG as judged by a larger concentration domain for coacervation and a high yield of LF recovered once mixed with β-LG A i.e. 80% against a maximum of 42% with β-LG B. At thermodynamic level, the interaction of LF with both β-LG isoforms exhibited complex exothermic binding isotherms with both enthalpic and entropic contributions.
publishDate 2015
dc.date.none.fl_str_mv 2015-06
2018-11-29T13:12:44Z
2018-11-29T13:12:44Z
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 0268005X
https://doi.org/10.1016/j.foodhyd.2015.02.027
http://www.locus.ufv.br/handle/123456789/22644
identifier_str_mv 0268005X
url https://doi.org/10.1016/j.foodhyd.2015.02.027
http://www.locus.ufv.br/handle/123456789/22644
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Volume 48, Pages 238- 247, June 2015
dc.rights.driver.fl_str_mv 2015 Elsevier Ltd. All rights reserved
info:eu-repo/semantics/openAccess
rights_invalid_str_mv 2015 Elsevier Ltd. All rights reserved
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv pdf
application/pdf
dc.publisher.none.fl_str_mv Food Hydrocolloids
publisher.none.fl_str_mv Food Hydrocolloids
dc.source.none.fl_str_mv reponame:LOCUS Repositório Institucional da UFV
instname:Universidade Federal de Viçosa (UFV)
instacron:UFV
instname_str Universidade Federal de Viçosa (UFV)
instacron_str UFV
institution UFV
reponame_str LOCUS Repositório Institucional da UFV
collection LOCUS Repositório Institucional da UFV
repository.name.fl_str_mv LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)
repository.mail.fl_str_mv fabiojreis@ufv.br
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