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Please use this identifier to cite or link to this item: http://hdl.handle.net/1843/40783
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dc.creatorCarla Eduarda Ladeira Silvapt_BR
dc.creatorEliara Acipreste Hudsonpt_BR
dc.creatorÁlvaro Javier Patiño Agudelopt_BR
dc.creatorLuis Henrique Mendes da Silvapt_BR
dc.creatorMaximiliano Soares Pintopt_BR
dc.creatorMaria do Carmo Hespanholpt_BR
dc.creatorFrederico Augusto Ribeiro Barrospt_BR
dc.creatorAna Clarissa dos Santos Pirespt_BR
dc.date.accessioned2022-04-05T13:38:15Z-
dc.date.available2022-04-05T13:38:15Z-
dc.date.issued2018-
dc.citation.volume11pt_BR
dc.citation.issue3pt_BR
dc.citation.spage610pt_BR
dc.citation.epage620pt_BR
dc.identifier.doihttps://doi.org/10.1007/s11947-017-2028-7pt_BR
dc.identifier.issn19355149pt_BR
dc.identifier.urihttp://hdl.handle.net/1843/40783-
dc.description.resumoThe 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.pt_BR
dc.description.sponsorshipCNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológicopt_BR
dc.description.sponsorshipFAPEMIG - Fundação de Amparo à Pesquisa do Estado de Minas Geraispt_BR
dc.description.sponsorshipCAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superiorpt_BR
dc.languageengpt_BR
dc.publisherUniversidade Federal de Minas Geraispt_BR
dc.publisher.countryBrasilpt_BR
dc.publisher.departmentICA - INSTITUTO DE CIÊNCIAS AGRÁRIASpt_BR
dc.publisher.initialsUFMGpt_BR
dc.relation.ispartofFood and Bioprocess Technologypt_BR
dc.rightsAcesso Restritopt_BR
dc.subject.otherLeite - Proteínaspt_BR
dc.subject.otherEspectroscopia de fluorescênciapt_BR
dc.subject.otherAlbuminapt_BR
dc.subject.otherEstequiometriapt_BR
dc.titleβ-Carotene and milk protein complexation: a thermodynamic approach and a photo stabilization studypt_BR
dc.typeArtigo de Periódicopt_BR
dc.url.externahttps://link.springer.com/article/10.1007/s11947-017-2028-7pt_BR
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