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https://hdl.handle.net/1822/61782
Título: | Design of β-lactoglobulin micro- and nanostructures by controlling gelation through physical variables |
Autor(es): | Simões, Lívia Souza Araújo, J. Vicente, A. A. Ramos, Óscar L. |
Palavras-chave: | Purification Bio-based structures Globular proteins Whey proteins Protein interaction Aggregation |
Data: | Mar-2020 |
Editora: | Elsevier 1 |
Revista: | Food Hydrocolloids |
Citação: | Simões, Lívia S; Araújo, J.; Vicente, António A.; Ramos, Óscar L., Design of β-lactoglobulin micro- and nanostructures by controlling gelation through physical variables. Food Hydrocolloids, 100(105357), 2020 |
Resumo(s): | β-lactoglobulin (β-Lg) is the major protein fraction of bovine whey serum and its principal gelling agent. Its gelation capacity enables conformational changes associated with protein-protein interactions that allow the design of structures with different properties and morphologies. Thus, the aim of this work was to successfully use β-Lg, purified from a commercial whey protein isolate, to develop food-grade micro- (with diameters between 200 and 300 nm) and nano- (with diameters ≤ 100 nm) structures. For this purpose, the phenomena involved in β-Lg gelation were studied under combined effects of concentrations (from 5 to 15 mg mL−1), heating temperature (from 60 to 80 °C) and heating time (from 5 to 25 min) for pH values of 3, 4, 6 and 7. The effects of such conditions on β-Lg structures were evaluated and the protein was fully characterized in terms of size, polydispersity index (PDI) and surface charge (by dynamic light scattering – DLS), morphology (by transmission electron microscopy - TEM) and conformational structure (circular dichroism, intrinsic and extrinsic fluorescence). Results have shown that β-Lg nanostructures were formed at pH 3 (with diameters between 12.1 and 22.3 nm) and at 7 (with diameters between 8.9 and 35.3 nm). At pH 4 structures were obtained at macroscale (i.e., ≥ 6 μm) for all β-Lg concentrations when heated at 70 and 80 °C, independent of the time of heating. For pH 6, it was possible to obtain β-Lg structures either at micro- (245.0 – 266.4 nm) or nanoscale (≤ 100 nm) with the lowest polydispersity (PDI) values (≤ 0.25), in accordance with TEM analyses, for heating at 80 °C for 15 min. Intrinsic and extrinsic fluorescence data and far-UV circular dichroism spectra measurements revealed conformational changes on β-Lg structure that support these evidences. A strict control of the physical and environmental conditions is crucial for developing β-Lg structures with the desired characteristics, thus calling for the understanding of the mechanisms of protein aggregation and intermolecular interaction when designing β-Lg structures with novel functionalities. |
Tipo: | Artigo |
URI: | https://hdl.handle.net/1822/61782 |
DOI: | 10.1016/j.foodhyd.2019.105357 |
ISSN: | 0268-005X |
e-ISSN: | 1873-7137 |
Versão da editora: | http://www.elsevier.com/locate/issn/0268005X |
Arbitragem científica: | yes |
Acesso: | Acesso aberto |
Aparece nas coleções: | CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series |
Ficheiros deste registo:
Ficheiro | Descrição | Tamanho | Formato | |
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document_51972_1.pdf | 2,54 MB | Adobe PDF | Ver/Abrir |