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dc.contributor.authorAn, B.en
dc.contributor.authorWu, X.en
dc.contributor.authorLi, M.en
dc.contributor.authorChen, Yijunen
dc.contributor.authorLi, F.en
dc.contributor.authorYan, X.en
dc.contributor.authorWang, Jialinen
dc.contributor.authorLi, C.en
dc.contributor.authorBrennan, Charles S.en
dc.date.accessioned2018-08-14T01:02:26Z
dc.date.available2016-10-25en
dc.date.issued2016-12en
dc.date.submitted2016-08-10en
dc.identifier.issn0950-5423en
dc.identifier.urihttps://hdl.handle.net/10182/10136
dc.description.abstractProtein fibrillation serves a broad range of biological functions from surface colonising to mechanically reinforcing structures; it is also associated with the development of neurodegenerative disorders. Although fibrillation is considered to be an inherent ability of polypeptides to form backbones, relevant studies have long concentrated on aqueous-soluble proteins rather than on insoluble structures. In this study, the self-assembly of hydrophobic proteins into amyloid nanofibrils was studied using α-zein as a model protein. The self-assembled morphologies of α-zein were determined by hydrophobic–hydrophilic characters of both the protein and the solvent. Upon thermally incubating in aqueous ethanol, α-zein formed amyloid nanofibrils with lower ethanol compositions and near-neutral pHs, while acidic conditions and high ethanol compositions result in the formation of spherical aggregations. The fibrillation of α-zein shows a great potential in serving as bio-based gels or reinforced fillers in food, cosmetic and pharmaceutical applications.en
dc.format.extent2621-2629en
dc.language.isoenen
dc.publisherWiley Online on behalf of the Institute of Food Science and Technologyen
dc.relationThe original publication is available from - Wiley Online on behalf of the Institute of Food Science and Technology - https://doi.org/10.1111/ijfs.13248en
dc.relation.urihttps://doi.org/10.1111/ijfs.13248en
dc.rights© 2016 Institute of Food Science and Technologyen
dc.subjectamyloid nanofibrilsen
dc.subjecthydrophobic interactionen
dc.subjectself-assembleen
dc.subjectα-zeinen
dc.subject-zeinen
dc.subjectFood Scienceen
dc.titleHydrophobicity-modulating self-assembled morphologies of α-zein in aqueous ethanolen
dc.typeJournal Article
lu.contributor.unitLincoln Universityen
lu.contributor.unitFaculty of Agriculture and Life Sciencesen
lu.contributor.unitDepartment of Wine, Food and Molecular Biosciencesen
dc.identifier.doi10.1111/ijfs.13248en
dc.relation.isPartOfInternational Journal of Food Science and Technologyen
pubs.issue12en
pubs.organisational-group/LU
pubs.organisational-group/LU/Agriculture and Life Sciences
pubs.organisational-group/LU/Agriculture and Life Sciences/WFMB
pubs.organisational-group/LU/Research Management Office
pubs.organisational-group/LU/Research Management Office/QE18
pubs.publication-statusPublisheden
pubs.volume51en
dc.identifier.eissn1365-2621en
lu.identifier.orcid0000-0003-2479-8478


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