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

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dc.creatorCarla Eduarda Ladeira Silva
dc.creatorEliara Acipreste Hudson
dc.creatorÁlvaro Javier Patiño Agudelo
dc.creatorLuis Henrique Mendes da Silva
dc.creatorMaximiliano Soares Pinto
dc.creatorMaria do Carmo Hespanhol
dc.creatorFrederico Augusto Ribeiro Barros
dc.creatorAna Clarissa dos Santos Pires
dc.date.accessioned2022-04-05T13:38:15Z
dc.date.accessioned2025-09-08T23:01:46Z
dc.date.available2022-04-05T13:38:15Z
dc.date.issued2018
dc.description.sponsorshipCNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológico
dc.description.sponsorshipFAPEMIG - Fundação de Amparo à Pesquisa do Estado de Minas Gerais
dc.description.sponsorshipCAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superior
dc.identifier.doihttps://doi.org/10.1007/s11947-017-2028-7
dc.identifier.issn19355149
dc.identifier.urihttps://hdl.handle.net/1843/40783
dc.languageeng
dc.publisherUniversidade Federal de Minas Gerais
dc.relation.ispartofFood and Bioprocess Technology
dc.rightsAcesso Restrito
dc.subjectLeite - Proteínas
dc.subjectEspectroscopia de fluorescência
dc.subjectAlbumina
dc.subjectEstequiometria
dc.titleβ-Carotene and milk protein complexation: a thermodynamic approach and a photo stabilization study
dc.typeArtigo de periódico
local.citation.epage620
local.citation.issue3
local.citation.spage610
local.citation.volume11
local.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.
local.publisher.countryBrasil
local.publisher.departmentICA - INSTITUTO DE CIÊNCIAS AGRÁRIAS
local.publisher.initialsUFMG
local.url.externahttps://link.springer.com/article/10.1007/s11947-017-2028-7

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