Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/352204
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dc.contributor.CRUESPUNIVERSIDADE ESTADUAL DE CAMPINASpt_BR
dc.contributor.authorunicampLeite Júnior, Bruno Ricardo de Castro-
dc.contributor.authorunicampRibeiro, Luma Rossi-
dc.contributor.authorunicampCristianini, Marcelo-
dc.typeArtigopt_BR
dc.titleEffect of dynamic high pressure on functional and structural properties of bovine serum albuminpt_BR
dc.contributor.authorMaresca, Paola-
dc.contributor.authorFerrari, Giovanna-
dc.contributor.authorLeite Júnior, Bruno Ricardo de Castro-
dc.contributor.authorZanphorlin, Leticia Maria-
dc.contributor.authorRibeiro, Luma Rossi-
dc.contributor.authorMurakami, Mário Tyago-
dc.contributor.authorCristianini, Marcelo-
dc.subjectProteínaspt_BR
dc.subject.otherlanguageProteinspt_BR
dc.description.abstractDynamic high pressure (DHP) has been investigated as an innovative suitable method to induce protein modifications. This work evaluated the effect of DHP (up to three passes at 100, 150 and 200 MPa, with an inlet temperature of 20 °C) on functional and structural properties of bovine serum albumin (BSA). Results indicated that DHP process applied up to an energy limit of 100 MPa increased the protein foaming capacity (FC) (p < 0.05 - increase up to 63% after 1 pass at 100 MPa) and the utilization of multiple passes at high pressure promoted a reduction in this property (p < 0.05 - reduction up to 31.6% after 3 passes at 200 MPa). Similar results were observed for sulfhydryl group, indicating an influence of free thiol groups on FC. Complementarily, DHP process promoted an increase of proteins particles size, suggesting a new rearrangement of their conformational structure. DHP did not affect tryptophan microenvironment in BSA; however, this process induced the rearrangement of secondary structure elements. In the first cycle, the pressure increase resulted in a loss of secondary structure, while in the second and third cycles the DHP process resulted in the gain of secondary structure elements. These results indicated that the second and third passes triggered a molecular rearrangement of the protein structure, giving rise to a novel and more stable conformational state. This conclusion was also supported by thermal unfolding studies (melting temperature reduction from 67.5 to 54.6 °C after 1 pass at 200 MPa), in which the additional cycles of DHP caused the occurrence of an initial denaturation at high temperatures, compared to the first cyclept_BR
dc.relation.ispartofFood research internationalpt_BR
dc.relation.ispartofabbreviationFood res. int.pt_BR
dc.publisher.cityOxfordpt_BR
dc.publisher.countryReino Unidopt_BR
dc.publisherElsevierpt_BR
dc.date.issued2017-
dc.date.monthofcirculationSept.pt_BR
dc.language.isoengpt_BR
dc.description.volume99pt_BR
dc.description.issuepart1pt_BR
dc.description.firstpage748pt_BR
dc.description.lastpage754pt_BR
dc.rightsFechadopt_BR
dc.sourceWOSpt_BR
dc.identifier.issn0963-9969pt_BR
dc.identifier.eissn1873-7145pt_BR
dc.identifier.doi10.1016/j.foodres.2017.06.047pt_BR
dc.identifier.urlhttps://www.sciencedirect.com/science/article/pii/S0963996917303010pt_BR
dc.description.sponsorshipFUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULO - FAPESPpt_BR
dc.description.sponsordocumentnumber2012/13509-6pt_BR
dc.date.available2020-11-11T21:27:22Z-
dc.date.accessioned2020-11-11T21:27:22Z-
dc.description.provenanceSubmitted by Thais de Brito Barroso (tbrito@unicamp.br) on 2020-11-11T21:27:22Z No. of bitstreams: 0en
dc.description.provenanceMade available in DSpace on 2020-11-11T21:27:22Z (GMT). No. of bitstreams: 0 Previous issue date: 2017en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/352204-
dc.contributor.departmentSem informaçãopt_BR
dc.contributor.departmentSem informaçãopt_BR
dc.contributor.departmentDepartamento de Tecnologia de Alimentospt_BR
dc.contributor.unidadeFaculdade de Engenharia de Alimentospt_BR
dc.contributor.unidadeFaculdade de Engenharia de Alimentospt_BR
dc.contributor.unidadeFaculdade de Engenharia de Alimentospt_BR
dc.subject.keywordHigh pressure homogenizationpt_BR
dc.subject.keywordBSApt_BR
dc.subject.keywordCircular dichroismpt_BR
dc.subject.keywordUnfoldingpt_BR
dc.identifier.source000409152200079pt_BR
dc.creator.orcid0000-0001-9030-2819pt_BR
dc.creator.orcid0000-0002-6305-9654pt_BR
dc.creator.orcid0000-0001-7740-0449pt_BR
dc.type.formArtigopt_BR
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