β-Carotene and milk protein complexation: a thermodynamic approach and a photo stabilization study

Detalhes bibliográficos
Autor(a) principal: Silva, Carla Eduarda Ladeira
Data de Publicação: 2017
Outros Autores: 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
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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spelling 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
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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
dc.rights.driver.fl_str_mv Springer US
info:eu-repo/semantics/openAccess
rights_invalid_str_mv Springer US
eu_rights_str_mv openAccess
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dc.publisher.none.fl_str_mv Food and Bioprocess Technology
publisher.none.fl_str_mv Food and Bioprocess Technology
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