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dc.contributor.authorDave, ACen_US
dc.contributor.authorLoveday, SMen_US
dc.contributor.authorAnema, SGen_US
dc.contributor.authorJameson, GBen_US
dc.contributor.authorSingh, Hen_US
dc.date.accessioned2014-11-25T19:54:05Z
dc.date.available2015-02-01en_US
dc.date.issued2015-02-01en_US
dc.identifierhttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000345507700012&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=c5bb3b2499afac691c2e3c1a83ef6fefen_US
dc.identifier.citationINTERNATIONAL DAIRY JOURNAL, 2015, 41 pp. 64 - 67 (4)en_US
dc.identifier.issn0958-6946en_US
dc.format.extent64 - 67 (4)en_US
dc.languageEnglishen_US
dc.publisherELSEVIER SCI LTDen_US
dc.relation.isreplacedby123456789/4817
dc.relation.isreplacedbyhttp://hdl.handle.net/123456789/4817
dc.rightsReleased with a Creative Commons Attribution Non-Commercial No Derivatives License
dc.subjectScience & Technologyen_US
dc.subjectLife Sciences & Biomedicineen_US
dc.subjectFood Science & Technologyen_US
dc.subjectHEAT-TREATMENTen_US
dc.subjectAGGREGATIONen_US
dc.subjectCONVERSIONen_US
dc.subjectMECHANISMen_US
dc.titleFormation of nano-fibrils from the A, B and C variants of bovine beta-lactoglobulinen_US
dc.typeJournal Article
dc.citation.volume41en_US
dc.identifier.doi10.1016/j.idairyj.2014.09.011en_US
dc.identifier.elements-id219551
dc.relation.isPartOfINTERNATIONAL DAIRY JOURNALen_US
dc.description.publication-statusPublisheden_US
dc.description.publication-statusPublisheden_US
dc.description.notesThis study investigated the self-assembly of purified β-lactoglobulin (β-Lg) genetic variants A, B and C into amyloid-like fibrils. β-Lg solutions (1%, w/v) were heated at 80 °C and pH 2 and were analysed for the presence of fibrils using the thioflavin T assay. Reducing sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) was used to follow heat-induced acid hydrolysis of β-Lg monomers. Fibrils separated from heated solutions were characterised by SDS-PAGE and transmission electron microscopy. The substitution of amino acid residues in β-Lg variants A, B and C did not significantly affect the kinetics of acid hydrolysis, self-assembly kinetics, or the morphology of the fibrils. The fibrils from β-Lg A, B and C were, however, slightly different in peptide compositions. These differences may be explained on the basis of amino acid substitutions, in particular the Asp64 of β-Lg A that is Gly in variants B and C.
dc.description.notesThis study investigated the self-assembly of purified β-lactoglobulin (β-Lg) genetic variants A, B and C into amyloid-like fibrils. β-Lg solutions (1%, w/v) were heated at 80 °C and pH 2 and were analysed for the presence of fibrils using the thioflavin T assay. Reducing sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) was used to follow heat-induced acid hydrolysis of β-Lg monomers. Fibrils separated from heated solutions were characterised by SDS-PAGE and transmission electron microscopy. The substitution of amino acid residues in β-Lg variants A, B and C did not significantly affect the kinetics of acid hydrolysis, self-assembly kinetics, or the morphology of the fibrils. The fibrils from β-Lg A, B and C were, however, slightly different in peptide compositions. These differences may be explained on the basis of amino acid substitutions, in particular the Asp64 of β-Lg A that is Gly in variants B and C.
pubs.organisational-group/Massey University
pubs.organisational-group/Massey University/College of Health
pubs.organisational-group/Massey University/College of Health/Food, Nutrition and Human Health
pubs.organisational-group/Massey University/College of Health/PVC's Office - College of Health
pubs.organisational-group/Massey University/College of Sciences
pubs.organisational-group/Massey University/College of Sciences/Institute of Fundamental Sciences
pubs.notesNot knownen_US


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