Produção Nacional
Revisado por pares
Formation and characterization of supramolecular structures of β-lactoglobulin and lactoferrin proteins
2017; Elsevier BV; Volume: 100; Linguagem: Inglês
10.1016/j.foodres.2017.07.065
ISSN1873-7145
AutoresCamila Santiago Saraiva, Jane Sélia dos Reis Coimbra, Álvaro Vianna Novaes de Carvalho Teixeira, Eduardo Basílio de Oliveira, Reinaldo F. Teófilo, Angélica Ribeiro da Costa, Éverton de Almeida Alves Barbosa,
Tópico(s)Infant Nutrition and Health
ResumoCombination 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 pH6.5 and at temperatures of 62.5°C. In those conditions, more stable systems with reduced hydrophobic surface and average sizes between 30 and 100nm were generated. The correlation between pH and temperature suggests that the method of preparation of the supramolecular structure affects its size during storage.
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