Selective coacervation between lactoferrin and the two isoforms of β-lactoglobulin
Autor(a) principal: | |
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Data de Publicação: | 2015 |
Outros Autores: | , , , |
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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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 |
_version_ |
1817559841713946624 |