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Formation and characterization of supramolecular structures of ß-lactoglobulin and lactoferrin proteins.
Saraiva, Camila Santiago; Dos Reis Coimbra, Jane Sélia; de Carvalho Teixeira, Alvaro Vianna Novaes; de Oliveira, Eduardo Basílio; Teófílo, Reinaldo Francisco; da Costa, Angélica Ribeiro; de Almeida Alves Barbosa, Éverton.
Afiliação
  • Saraiva CS; Universidade Federal de Viçosa, Departamento de Tecnologia de Alimentos, Campus Universitário S/N, 36570-000 Viçosa, Minas Gerais, Brazil.
  • Dos Reis Coimbra JS; Universidade Federal de Viçosa, Departamento de Tecnologia de Alimentos, Campus Universitário S/N, 36570-000 Viçosa, Minas Gerais, Brazil. Electronic address: jcoimbra@ufv.br.
  • de Carvalho Teixeira AVN; Universidade Federal de Viçosa, Departamento de Física, Campus Universitário S/N, 36570-000 Viçosa, Minas Gerais, Brazil.
  • de Oliveira EB; Universidade Federal de Viçosa, Departamento de Tecnologia de Alimentos, Campus Universitário S/N, 36570-000 Viçosa, Minas Gerais, Brazil.
  • Teófílo RF; Universidade Federal de Viçosa, Departamento de Química, Campus Universitário S/N, 36570-000 Viçosa, Minas Gerais, Brazil.
  • da Costa AR; Universidade Federal de Viçosa, Departamento de Tecnologia de Alimentos, Campus Universitário S/N, 36570-000 Viçosa, Minas Gerais, Brazil.
  • de Almeida Alves Barbosa É; Universidade Federal de Viçosa, Departamento de Bioquímica e Biologia Molecular, Campus Universitário S/N, 36570-000 Viçosa, Minas Gerais, Brazil.
Food Res Int ; 100(Pt 1): 674-681, 2017 10.
Article em En | MEDLINE | ID: mdl-28873736
Combination of ß-lactoglobulin (ß-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 ß-Lg and around 52°C and 85°C (a small portion) for the Lf. The protein molar ratio of 2:1 Lf/ß-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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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Complexos Multiproteicos / Lactoferrina / Lactoglobulinas Limite: Animals Idioma: En Revista: Food Res Int Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Brasil País de publicação: Canadá

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Complexos Multiproteicos / Lactoferrina / Lactoglobulinas Limite: Animals Idioma: En Revista: Food Res Int Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Brasil País de publicação: Canadá