pH- and ionic strength-dependent interaction between cyanidin-3-O-glucoside and sodium caseinate
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | LOCUS Repositório Institucional da UFV |
Texto Completo: | https://doi.org/10.1016/j.foodchem.2017.06.081 http://www.locus.ufv.br/handle/123456789/21230 |
Resumo: | Understanding the mechanism of interaction between food proteins and bioactives constitutes the preliminary step to design food grade nanocarriers. We investigated the interaction between cyanidin-3-O-glucoside (C3G), and 20 nm-sized sodium caseinate nanoparticles (NaCas) at pH 7 and pH 2 by fluorescence spectroscopy and dynamic light scattering. The characterization of the C3G-NaCas interaction indicated that the fluorescence quenching mechanism was predominantly static. C3G interacted with two sets of binding sites with association constants Ka of 106 and 105 M−1. Electrostatic interactions dominated at pH 7, while hydrophobic effects were the main force at pH 2. Interestingly, the two sets of binding sites were discriminated by ionic strength at pH 7. The binding of C3G slightly modified the average diameter of NaCas nanoparticles without alteration of its surface charge suggesting a complexation of C3G molecules in the internal casein structure. Thus, NaCas constitutes a putative nanocarrier for anthocyanins in new functional foods. |
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Casanova, FedericoChapeau, Anne-LaureHamon, PascalineCarvalho, Antonio F. deCroguennec, ThomasBouhallab, Saïd2018-08-20T18:17:44Z2018-08-20T18:17:44Z2018-11-3003088146https://doi.org/10.1016/j.foodchem.2017.06.081http://www.locus.ufv.br/handle/123456789/21230Understanding the mechanism of interaction between food proteins and bioactives constitutes the preliminary step to design food grade nanocarriers. We investigated the interaction between cyanidin-3-O-glucoside (C3G), and 20 nm-sized sodium caseinate nanoparticles (NaCas) at pH 7 and pH 2 by fluorescence spectroscopy and dynamic light scattering. The characterization of the C3G-NaCas interaction indicated that the fluorescence quenching mechanism was predominantly static. C3G interacted with two sets of binding sites with association constants Ka of 106 and 105 M−1. Electrostatic interactions dominated at pH 7, while hydrophobic effects were the main force at pH 2. Interestingly, the two sets of binding sites were discriminated by ionic strength at pH 7. The binding of C3G slightly modified the average diameter of NaCas nanoparticles without alteration of its surface charge suggesting a complexation of C3G molecules in the internal casein structure. Thus, NaCas constitutes a putative nanocarrier for anthocyanins in new functional foods.engFood Chemistryv. 267, p. 52- 59, november 2018Elsevier Ltd.info:eu-repo/semantics/openAccessCyanidin-3-O-glucosideSodium caseinateFluorescence spectroscopyInteractionThermodynamic analysispH- and ionic strength-dependent interaction between cyanidin-3-O-glucoside and sodium caseinateinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINALartigo.pdfartigo.pdfTexto completoapplication/pdf960530https://locus.ufv.br//bitstream/123456789/21230/1/artigo.pdfc66edce2e410871fca3199464af4e255MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/21230/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52THUMBNAILartigo.pdf.jpgartigo.pdf.jpgIM Thumbnailimage/jpeg5195https://locus.ufv.br//bitstream/123456789/21230/3/artigo.pdf.jpgb7f211043f9ceb5f84160f871349e5f2MD53123456789/212302018-08-20 23:00:44.529oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452018-08-21T02:00:44LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false |
dc.title.en.fl_str_mv |
pH- and ionic strength-dependent interaction between cyanidin-3-O-glucoside and sodium caseinate |
title |
pH- and ionic strength-dependent interaction between cyanidin-3-O-glucoside and sodium caseinate |
spellingShingle |
pH- and ionic strength-dependent interaction between cyanidin-3-O-glucoside and sodium caseinate Casanova, Federico Cyanidin-3-O-glucoside Sodium caseinate Fluorescence spectroscopy Interaction Thermodynamic analysis |
title_short |
pH- and ionic strength-dependent interaction between cyanidin-3-O-glucoside and sodium caseinate |
title_full |
pH- and ionic strength-dependent interaction between cyanidin-3-O-glucoside and sodium caseinate |
title_fullStr |
pH- and ionic strength-dependent interaction between cyanidin-3-O-glucoside and sodium caseinate |
title_full_unstemmed |
pH- and ionic strength-dependent interaction between cyanidin-3-O-glucoside and sodium caseinate |
title_sort |
pH- and ionic strength-dependent interaction between cyanidin-3-O-glucoside and sodium caseinate |
author |
Casanova, Federico |
author_facet |
Casanova, Federico Chapeau, Anne-Laure Hamon, Pascaline Carvalho, Antonio F. de Croguennec, Thomas Bouhallab, Saïd |
author_role |
author |
author2 |
Chapeau, Anne-Laure Hamon, Pascaline Carvalho, Antonio F. de Croguennec, Thomas Bouhallab, Saïd |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Casanova, Federico Chapeau, Anne-Laure Hamon, Pascaline Carvalho, Antonio F. de Croguennec, Thomas Bouhallab, Saïd |
dc.subject.pt-BR.fl_str_mv |
Cyanidin-3-O-glucoside Sodium caseinate Fluorescence spectroscopy Interaction Thermodynamic analysis |
topic |
Cyanidin-3-O-glucoside Sodium caseinate Fluorescence spectroscopy Interaction Thermodynamic analysis |
description |
Understanding the mechanism of interaction between food proteins and bioactives constitutes the preliminary step to design food grade nanocarriers. We investigated the interaction between cyanidin-3-O-glucoside (C3G), and 20 nm-sized sodium caseinate nanoparticles (NaCas) at pH 7 and pH 2 by fluorescence spectroscopy and dynamic light scattering. The characterization of the C3G-NaCas interaction indicated that the fluorescence quenching mechanism was predominantly static. C3G interacted with two sets of binding sites with association constants Ka of 106 and 105 M−1. Electrostatic interactions dominated at pH 7, while hydrophobic effects were the main force at pH 2. Interestingly, the two sets of binding sites were discriminated by ionic strength at pH 7. The binding of C3G slightly modified the average diameter of NaCas nanoparticles without alteration of its surface charge suggesting a complexation of C3G molecules in the internal casein structure. Thus, NaCas constitutes a putative nanocarrier for anthocyanins in new functional foods. |
publishDate |
2018 |
dc.date.accessioned.fl_str_mv |
2018-08-20T18:17:44Z |
dc.date.available.fl_str_mv |
2018-08-20T18:17:44Z |
dc.date.issued.fl_str_mv |
2018-11-30 |
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.foodchem.2017.06.081 http://www.locus.ufv.br/handle/123456789/21230 |
dc.identifier.issn.none.fl_str_mv |
03088146 |
identifier_str_mv |
03088146 |
url |
https://doi.org/10.1016/j.foodchem.2017.06.081 http://www.locus.ufv.br/handle/123456789/21230 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartofseries.pt-BR.fl_str_mv |
v. 267, p. 52- 59, november 2018 |
dc.rights.driver.fl_str_mv |
Elsevier Ltd. info:eu-repo/semantics/openAccess |
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Elsevier Ltd. |
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openAccess |
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application/pdf |
dc.publisher.none.fl_str_mv |
Food Chemistry |
publisher.none.fl_str_mv |
Food Chemistry |
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LOCUS Repositório Institucional da UFV |
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