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https://locus.ufv.br//handle/123456789/19706
Tipo: | Artigo |
Título: | Formation and characterization of supramolecular structures of β-lactoglobulin and lactoferrin proteins |
Autor(es): | Saraiva, Camila Santiago Coimbra, Jane Sélia dos Reis Teixeira, Alvaro Vianna Novaes de Carvalho Oliveira, Eduardo Basílio de Teófílo, Reinaldo Francisco Costa, Angélica Ribeiro da Barbosa, Éverton de Almeida Alves |
Abstract: | Combination 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. |
Palavras-chave: | Acidification Calorimetry Gelation Heating Molecular interaction Self-assembly |
Editor: | Food Research International |
Tipo de Acesso: | Elsevier Ltd. |
URI: | https://doi.org/10.1016/j.foodres.2017.07.065 http://www.locus.ufv.br/handle/123456789/19706 |
Data do documento: | 29-Jul-2017 |
Aparece nas coleções: | Artigos |
Arquivos associados a este item:
Arquivo | Descrição | Tamanho | Formato | |
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artigo.pdf Until 2100-12-31 | texto completo | 1,04 MB | Adobe PDF | Visualizar/Abrir ACESSO RESTRITO |
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