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https://hdl.handle.net/1822/61782
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Campo DC | Valor | Idioma |
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dc.contributor.author | Simões, Lívia Souza | por |
dc.contributor.author | Araújo, J. | por |
dc.contributor.author | Vicente, A. A. | por |
dc.contributor.author | Ramos, Óscar L. | por |
dc.date.accessioned | 2019-10-14T09:34:58Z | - |
dc.date.available | 2019-10-14T09:34:58Z | - |
dc.date.issued | 2020-03 | - |
dc.identifier.citation | 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 | por |
dc.identifier.issn | 0268-005X | por |
dc.identifier.uri | https://hdl.handle.net/1822/61782 | - |
dc.description.abstract | 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. | por |
dc.description.sponsorship | Lívia de Souza Simões gratefully acknowledges her grant to CNPq (Conselho Nacional de Desenvolvimento Científico e Tecnológico, Brasil) from Brazil. Oscar L. Ramos gratefully acknowledges the Fundação para a Ciência e Tecnologia (FCT, Portugal) for his fellowship (SFRH/BPD/80766/2011). The authors also would like to acknowledge Ana I. Bourbon, from the International Iberian Nanotechnology Laboratory, for assistance in native polyacrylamide gel electrophoresis. This study was supported by the FCT under the scope of the strategic funding of UID/BIO/04469 unit and COMPETE 2020 (POCI-01-0145-FEDER-006684) and BioTecNorte operation (NORTE-01-0145-FEDER-000004) funded by the European Regional Development Fund under the scope of Norte2020 - Programa Operacional Regional do Norte, Portugal. | por |
dc.language.iso | eng | por |
dc.publisher | Elsevier 1 | por |
dc.relation | info:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBPD%2F80766%2F2011/PT | por |
dc.relation | info:eu-repo/grantAgreement/FCT/5876/147337/PT | por |
dc.rights | openAccess | por |
dc.subject | Purification | por |
dc.subject | Bio-based structures | por |
dc.subject | Globular proteins | por |
dc.subject | Whey proteins | por |
dc.subject | Protein interaction | por |
dc.subject | Aggregation | por |
dc.title | Design of β-lactoglobulin micro- and nanostructures by controlling gelation through physical variables | por |
dc.type | article | - |
dc.peerreviewed | yes | por |
dc.relation.publisherversion | http://www.elsevier.com/locate/issn/0268005X | por |
dc.comments | CEB51972 | por |
oaire.citationVolume | 100 | por |
dc.date.updated | 2019-09-28T12:36:15Z | - |
dc.identifier.eissn | 1873-7137 | por |
dc.identifier.doi | 10.1016/j.foodhyd.2019.105357 | por |
dc.description.publicationversion | info:eu-repo/semantics/publishedVersion | - |
dc.subject.wos | Science & Technology | por |
sdum.journal | Food Hydrocolloids | por |
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 |