Formation and characterization of supramolecular structures of β-lactoglobulin and lactoferrin proteins
| Autor: | Jane Sélia dos Reis Coimbra, Eduardo Basílio de Oliveira, Angélica Ribeiro da Costa, Camila Santiago Saraiva, Alvaro Vianna Novaes de Carvalho Teixeira, Éverton de Almeida Alves Barbosa, Reinaldo F. Teófilo |
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| Rok vydání: | 2017 |
| Předmět: |
Circular dichroism
Gelation Hot Temperature Structure formation Supramolecular chemistry Lactoglobulins 02 engineering and technology Calorimetry Acidification Heating 0404 agricultural biotechnology Differential scanning calorimetry Dynamic light scattering Zeta potential Animals Calorimetry Differential Scanning Protein Stability Chemistry Spectrum Analysis Molecular interaction Self-assembly 04 agricultural and veterinary sciences 021001 nanoscience & nanotechnology 040401 food science Lactoferrin Crystallography Multiprotein Complexes Cattle 0210 nano-technology Hydrophobic and Hydrophilic Interactions Food Science |
| Zdroj: | LOCUS Repositório Institucional da UFV Universidade Federal de Viçosa (UFV) instacron:UFV |
| ISSN: | 0963-9969 |
| DOI: | 10.1016/j.foodres.2017.07.065 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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