Formation and characterization of supramolecular structures of β-lactoglobulin and lactoferrin proteins

dc.creatorSaraiva, Camila Santiago
dc.creatorCoimbra, Jane Sélia dos Reis
dc.creatorTeixeira, Alvaro Vianna Novaes de Carvalho
dc.creatorOliveira, Eduardo Basílio de
dc.creatorTeófílo, Reinaldo Francisco
dc.creatorCosta, Angélica Ribeiro da
dc.creatorBarbosa, Éverton de Almeida Alves
dc.date2018-05-18T15:47:55Z
dc.date2018-05-18T15:47:55Z
dc.date2017-07-29
dc.date.accessioned2023-09-27T21:04:30Z
dc.date.available2023-09-27T21:04:30Z
dc.identifier09639969
dc.identifierhttps://doi.org/10.1016/j.foodres.2017.07.065
dc.identifierhttp://www.locus.ufv.br/handle/123456789/19706
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8954036
dc.descriptionCombination of β-lactoglobulin (β-Lg) and lactoferrin (Lf), biomacromolecules derived from bovine whey, was used in the formation of supramolecular structures by thermal gelation technique to adjust the pH. Furthermore, the influence of the molar ratio, temperature, pH, and heating time in the formation of supramolecular structures were also studied. The characterization of the protein supramolecular structures was performed using dynamic light scattering, zeta potential measurements, molecular spectrofluorimetry, and circular dichroism spectroscopy. The thermal behavior of the pure proteins was investigated by differential scanning calorimetry. The protein denaturation temperatures were of around 85 °C for the β-Lg and around 52 °C and 85 °C (a small portion) for the Lf. The protein molar ratio of 2:1 Lf/β-Lg was used to form the structures, whose characterization showed that the best conditions of supramolecular structure formation occurred at pH 6.5 and at temperatures of 62.5 °C. In those conditions, more stable systems with reduced hydrophobic surface and average sizes between 30 and 100 nm were generated. The correlation between pH and temperature suggests that the method of preparation of the supramolecular structure affects its size during storage.
dc.formatpdf
dc.formatapplication/pdf
dc.languageeng
dc.publisherFood Research International
dc.relationv. 100, Part. 1, p. 674-681, Outubro 2017
dc.rightsElsevier Ltd.
dc.subjectAcidification
dc.subjectCalorimetry
dc.subjectGelation
dc.subjectHeating
dc.subjectMolecular interaction
dc.subjectSelf-assembly
dc.titleFormation and characterization of supramolecular structures of β-lactoglobulin and lactoferrin proteins
dc.typeArtigo


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