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Design of β-lactoglobulin micro- and nanostructures by controlling gelation through physical variables

2020Journal article Open access
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dc.contributor.authorSimões, Lívia S.
dc.contributor.authorAraújo, João F.
dc.contributor.authorVicente, António A.
dc.contributor.authorRamos, Oscar L.
dc.date.accessioned2019-10-21T13:51:40Z
dc.date.available2019-10-21T13:51:40Z
dc.date.issued2020
dc.description.abstractβ-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.pt_PT
dc.description.versioninfo:eu-repo/semantics/acceptedVersionpt_PT
dc.identifier.citationSimões, L. S., Araújo, J. F., Vicente, A. A., & Ramos, O. L. (2020). Design of β-lactoglobulin micro- and nanostructures by controlling gelation through physical variables. Food Hydrocolloids, 100, 105357. https://doi.org/10.1016/j.foodhyd.2019.105357pt_PT
dc.identifier.doi10.1016/j.foodhyd.2019.105357pt_PT
dc.identifier.eid85072311880
dc.identifier.eissn1873-7137
dc.identifier.issn0268-005X
dc.identifier.urihttp://hdl.handle.net/10400.14/28447
dc.identifier.wos000499650900014
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherElsevierpt_PT
dc.relationNORTE-01-0145-FEDER-000004
dc.relationINNOVATIVE FOOD-GRADE NANOSYSTEMS FOR THERAPEUTICAL FOOD PRODUCTS
dc.subjectPurificationpt_PT
dc.subjectBio-based structurespt_PT
dc.subjectGlobular proteinspt_PT
dc.subjectWhey proteinspt_PT
dc.subjectProtein interactionpt_PT
dc.subjectAggregationpt_PT
dc.titleDesign of β-lactoglobulin micro- and nanostructures by controlling gelation through physical variablespt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleINNOVATIVE FOOD-GRADE NANOSYSTEMS FOR THERAPEUTICAL FOOD PRODUCTS
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBPD%2F80766%2F2011/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/5876/UID%2FBIO%2F04469%2F2013/PT
oaire.citation.titleFood Hydrocolloidspt_PT
oaire.citation.volume100
oaire.fundingStream5876
person.familyNameFernandes Araújo
person.familyNameVicente
person.familyNameRamos
person.givenNameJoão
person.givenNameAntónio
person.givenNameOscar
person.identifier175018
person.identifier.ciencia-idDA1B-0AB7-5B8B
person.identifier.ciencia-idB112-A77C-62CC
person.identifier.ciencia-id5C19-49E0-96EF
person.identifier.orcid0000-0003-2797-1109
person.identifier.orcid0000-0003-3593-8878
person.identifier.orcid0000-0002-7627-189X
person.identifier.ridH-1555-2013
person.identifier.ridM-3981-2013
person.identifier.scopus-author-id57211033101
person.identifier.scopus-author-id7005820757
person.identifier.scopus-author-id54889028400
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
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relation.isAuthorOfPublication1f961d74-053d-4db3-a2f9-14bf3650aed2
relation.isAuthorOfPublication963e34eb-0799-48e9-ad87-c231a69c378d
relation.isAuthorOfPublication.latestForDiscovery1f961d74-053d-4db3-a2f9-14bf3650aed2
relation.isProjectOfPublication369b220c-2348-4482-b406-9a1f08594224
relation.isProjectOfPublication41185161-831e-42bd-b785-5a7ee240a2d2
relation.isProjectOfPublication.latestForDiscovery41185161-831e-42bd-b785-5a7ee240a2d2

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