β-Carotene and milk protein complexation: a thermodynamic approach and a photo stabilization study
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | LOCUS Repositório Institucional da UFV |
Texto Completo: | http://dx.doi.org/10.1007/s11947-017-2028-7 http://www.locus.ufv.br/handle/123456789/21704 |
Resumo: | The demand for bioactive molecules, such as β-carotene (β-car), has increased, but some characteristics such as low water solubility and low photo stability limit its application in many formulations. The bioactive entrapment into milk proteins may overcome this barrier. Thus, the aim of this work was to study the interaction between β-car and bovine serum albumin (BSA) or β-casein and the photo stability of this bioactive in the presence of the proteins. Fluorescence spectroscopy showed that at pH 7.0, increasing concentrations of β-carotene reduced the fluorescence intensity of both proteins, and the fluorescence-quenching mechanism is mainly static. The stoichiometry of the β-car/protein complex varied between proteins, being 1:1 to native BSA, 1:3 to denatured BSA (d-BSA), and 1:2 for β-casein. The standard Gibbs-free energy (ΔG°) of complex formation was negative for all systems studied and followed the order ΔG°BSA < ΔG°β-casein < ΔG°d-BSA. The formation of β-car/protein complex was driven by entropy increasing in all studied conditions. Both proteins improved β-car photo stability, but β-casein micelle was more efficient, reducing and increasing four times, respectively, the bioactive degradation constant and the half-time of β-car. The overall results pointed to the strategic use of milk proteins, especially β-casein micelles as nanovehicle for β-car in food and other systems. |
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Silva, Carla Eduarda LadeiraHudson, Eliara AcipresteAgudelo, Álvaro Javier PatiñoSilva, Luis Henrique Mendes daHespanhol, Maria do CarmoBarros, Frederico Augusto RibeiroPires, Ana Clarissa dos SantosPinto, Maximiliano Soares2018-09-09T22:30:04Z2018-09-09T22:30:04Z2017-12-021935-5149http://dx.doi.org/10.1007/s11947-017-2028-7http://www.locus.ufv.br/handle/123456789/21704The demand for bioactive molecules, such as β-carotene (β-car), has increased, but some characteristics such as low water solubility and low photo stability limit its application in many formulations. The bioactive entrapment into milk proteins may overcome this barrier. Thus, the aim of this work was to study the interaction between β-car and bovine serum albumin (BSA) or β-casein and the photo stability of this bioactive in the presence of the proteins. Fluorescence spectroscopy showed that at pH 7.0, increasing concentrations of β-carotene reduced the fluorescence intensity of both proteins, and the fluorescence-quenching mechanism is mainly static. The stoichiometry of the β-car/protein complex varied between proteins, being 1:1 to native BSA, 1:3 to denatured BSA (d-BSA), and 1:2 for β-casein. The standard Gibbs-free energy (ΔG°) of complex formation was negative for all systems studied and followed the order ΔG°BSA < ΔG°β-casein < ΔG°d-BSA. The formation of β-car/protein complex was driven by entropy increasing in all studied conditions. Both proteins improved β-car photo stability, but β-casein micelle was more efficient, reducing and increasing four times, respectively, the bioactive degradation constant and the half-time of β-car. The overall results pointed to the strategic use of milk proteins, especially β-casein micelles as nanovehicle for β-car in food and other systems.engFood and Bioprocess TechnologyVolume 11, Issue 3, P. 610–620, March 2018Springer USinfo:eu-repo/semantics/openAccessβ-CarBSAβ-CaseinFluorescence spectroscopyPhoto stabilityβ-Carotene and milk protein complexation: a thermodynamic approach and a photo stabilization studyinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINALartigo.pdfartigo.pdfTexto completoapplication/pdf994156https://locus.ufv.br//bitstream/123456789/21704/1/artigo.pdfaef12b29ce0dc03b871984d38c2d8eabMD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/21704/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52THUMBNAILartigo.pdf.jpgartigo.pdf.jpgIM Thumbnailimage/jpeg5102https://locus.ufv.br//bitstream/123456789/21704/3/artigo.pdf.jpg35b39641f175d8abbd08dfda2280f3e7MD53123456789/217042018-09-09 23:00:35.67oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452018-09-10T02:00:35LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false |
dc.title.en.fl_str_mv |
β-Carotene and milk protein complexation: a thermodynamic approach and a photo stabilization study |
title |
β-Carotene and milk protein complexation: a thermodynamic approach and a photo stabilization study |
spellingShingle |
β-Carotene and milk protein complexation: a thermodynamic approach and a photo stabilization study Silva, Carla Eduarda Ladeira β-Car BSA β-Casein Fluorescence spectroscopy Photo stability |
title_short |
β-Carotene and milk protein complexation: a thermodynamic approach and a photo stabilization study |
title_full |
β-Carotene and milk protein complexation: a thermodynamic approach and a photo stabilization study |
title_fullStr |
β-Carotene and milk protein complexation: a thermodynamic approach and a photo stabilization study |
title_full_unstemmed |
β-Carotene and milk protein complexation: a thermodynamic approach and a photo stabilization study |
title_sort |
β-Carotene and milk protein complexation: a thermodynamic approach and a photo stabilization study |
author |
Silva, Carla Eduarda Ladeira |
author_facet |
Silva, Carla Eduarda Ladeira Hudson, Eliara Acipreste Agudelo, Álvaro Javier Patiño Silva, Luis Henrique Mendes da Hespanhol, Maria do Carmo Barros, Frederico Augusto Ribeiro Pires, Ana Clarissa dos Santos Pinto, Maximiliano Soares |
author_role |
author |
author2 |
Hudson, Eliara Acipreste Agudelo, Álvaro Javier Patiño Silva, Luis Henrique Mendes da Hespanhol, Maria do Carmo Barros, Frederico Augusto Ribeiro Pires, Ana Clarissa dos Santos Pinto, Maximiliano Soares |
author2_role |
author author author author author author author |
dc.contributor.author.fl_str_mv |
Silva, Carla Eduarda Ladeira Hudson, Eliara Acipreste Agudelo, Álvaro Javier Patiño Silva, Luis Henrique Mendes da Hespanhol, Maria do Carmo Barros, Frederico Augusto Ribeiro Pires, Ana Clarissa dos Santos Pinto, Maximiliano Soares |
dc.subject.pt-BR.fl_str_mv |
β-Car BSA β-Casein Fluorescence spectroscopy Photo stability |
topic |
β-Car BSA β-Casein Fluorescence spectroscopy Photo stability |
description |
The demand for bioactive molecules, such as β-carotene (β-car), has increased, but some characteristics such as low water solubility and low photo stability limit its application in many formulations. The bioactive entrapment into milk proteins may overcome this barrier. Thus, the aim of this work was to study the interaction between β-car and bovine serum albumin (BSA) or β-casein and the photo stability of this bioactive in the presence of the proteins. Fluorescence spectroscopy showed that at pH 7.0, increasing concentrations of β-carotene reduced the fluorescence intensity of both proteins, and the fluorescence-quenching mechanism is mainly static. The stoichiometry of the β-car/protein complex varied between proteins, being 1:1 to native BSA, 1:3 to denatured BSA (d-BSA), and 1:2 for β-casein. The standard Gibbs-free energy (ΔG°) of complex formation was negative for all systems studied and followed the order ΔG°BSA < ΔG°β-casein < ΔG°d-BSA. The formation of β-car/protein complex was driven by entropy increasing in all studied conditions. Both proteins improved β-car photo stability, but β-casein micelle was more efficient, reducing and increasing four times, respectively, the bioactive degradation constant and the half-time of β-car. The overall results pointed to the strategic use of milk proteins, especially β-casein micelles as nanovehicle for β-car in food and other systems. |
publishDate |
2017 |
dc.date.issued.fl_str_mv |
2017-12-02 |
dc.date.accessioned.fl_str_mv |
2018-09-09T22:30:04Z |
dc.date.available.fl_str_mv |
2018-09-09T22:30:04Z |
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://dx.doi.org/10.1007/s11947-017-2028-7 http://www.locus.ufv.br/handle/123456789/21704 |
dc.identifier.issn.none.fl_str_mv |
1935-5149 |
identifier_str_mv |
1935-5149 |
url |
http://dx.doi.org/10.1007/s11947-017-2028-7 http://www.locus.ufv.br/handle/123456789/21704 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartofseries.pt-BR.fl_str_mv |
Volume 11, Issue 3, P. 610–620, March 2018 |
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Springer US info:eu-repo/semantics/openAccess |
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Springer US |
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openAccess |
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Food and Bioprocess Technology |
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Food and Bioprocess Technology |
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