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dc.contributor.CRUESPUNIVERSIDADE DE ESTADUAL DE CAMPINASpt_BR
dc.identifier.isbn1873-7137pt
dc.typeArtigo de Periódicopt_BR
dc.titleFormation And Ph-stability Of Whey Protein Fibrils In The Presence Of Lecithinpt_BR
dc.contributor.authorMantovanipt_BR
dc.contributor.authorRA; Fattoript_BR
dc.contributor.authorJ; Michelonpt_BR
dc.contributor.authorM; Cunhapt_BR
dc.contributor.authorRLpt_BR
unicamp.author.emailrosiane@unicamp.brpt_BR
dc.subjectWhey Proteinpt_BR
dc.subjectLecithinpt_BR
dc.subjectSurfactantpt_BR
dc.subjectSelf-assemblypt_BR
dc.subjectFibrilpt_BR
dc.subjectPh-stabilitypt_BR
dc.description.abstractThe effect of the soybean lecithin (SL) (0-0.25% w/v) on the kinetics of whey protein (2% w/v) fibrils formation and their stability under different pH values were evaluated. Linear and long fibrils were formed in the presence of SL at concentrations below critical micelle concentration whilst a higher SL content led to fibrils aggregation. The electrophoretic profiles and rate of fibril formation were not affected by the presence of SL. In spite of indicating SL-protein interaction, circular dichroism results showed that SL did not affect significantly the protein secondary structure conformation during heating. The pH-stability of fibrils was evaluated in a pH range from 3 to 7. At pH 3, the fibrils were isolated, but the increase of pH to 5 led to the formation of big aggregates that became more opened at pH 7, mainly in the presence of SL. These results were confirmed by small-angle X-ray scattering profiles. Different from fibrils formed without SL, the secondary structure of fibrils formed in the presence of SL showed no differences increasing pH from 3 to 7. Thus, despite not affecting the fibril growth mechanism and conformation, the presence of SL decreased the protein susceptibility to pH changes broadening the potential application of nanofibrils as a food ingredient. In this context, changes of process variables were carried out in order to enhance whey protein nanofibril formation in the presence of lecithin. Alternatives such as increasing pH, reducing protein-lecithin ratio and the modification of phospholipids composition favored the amyloid-like structure formation. (C) 2016 Elsevier Ltd. All rights reserved.en
dc.relation.ispartofFood Hydrocolloidspt_BR
dc.publisher.cityOXFORDpt_BR
dc.publisherELSEVIER SCI LTDpt_BR
dc.date.issued2016pt_BR
dc.identifier.citationFood Hydrocolloids. ELSEVIER SCI LTD, n. 60, p. 288 - 298.pt_BR
dc.language.isoEnglishpt_BR
dc.description.volume60pt_BR
dc.description.issuenumberpt_BR
dc.description.initialpage288pt_BR
dc.description.lastpage298pt_BR
dc.rightsfechadopt_BR
dc.sourceWOSpt_BR
dc.identifier.issn0268-005Xpt_BR
dc.identifier.wosidWOS:000377304700032pt_BR
dc.identifier.doi10.1016/j.foodhyd.2016.03.039pt_BR
dc.identifier.urlhttp://www-sciencedirect-com.ez88.periodicos.capes.gov.br/science/article/pii/S0268005X16301291pt_BR
dc.description.sponsorshipCAPES/FCT [349/13]pt_BR
dc.description.sponsorship1Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)pt_BR
dc.date.available2016-12-06T18:30:05Z-
dc.date.accessioned2016-12-06T18:30:05Z-
dc.description.provenanceMade available in DSpace on 2016-12-06T18:30:05Z (GMT). No. of bitstreams: 1 000377304700032.pdf: 1628455 bytes, checksum: 875c3e7e7e01065477118d92598b16b2 (MD5) Previous issue date: 2016en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/319952-
dc.description.conferencenomenullpt_BR
dc.description.conferencedatenullpt_BR
dc.description.conferencelocationpt_BR
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