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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/34976
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dc.contributor.authorde Assis, S. A.-
dc.contributor.authorFerreira, B. S.-
dc.contributor.authorFernandes, P.-
dc.contributor.authorGuaglianoni, D. G.-
dc.contributor.authorCabral, JMS-
dc.contributor.authorOliveira, OMMF-
dc.date.accessioned2014-05-20T15:24:21Z-
dc.date.accessioned2016-10-25T17:58:32Z-
dc.date.available2014-05-20T15:24:21Z-
dc.date.available2016-10-25T17:58:32Z-
dc.date.issued2004-07-01-
dc.identifierhttp://dx.doi.org/10.1016/j.foodchem.2003.09.040-
dc.identifier.citationFood Chemistry. Oxford: Elsevier B.V., v. 86, n. 3, p. 333-337, 2004.-
dc.identifier.issn0308-8146-
dc.identifier.urihttp://hdl.handle.net/11449/34976-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/34976-
dc.description.abstractThe optimum conditions for the production of low methoxyl pectin using pectinmethylesterase (PME) from acerola (Malpighia glabra L.), immobilized in gelatin, have been established by factorial design and response surface methodology. In the case of the free enzymes the optimum conditions for activity, within ranges adequate for food processing, are low NaCl concentrations (0.10 M), relatively high temperatures (55 degreesC) and slightly basic pH values (pH = 9). The temperature and pH seem to have strong influence on the observed activity. In the immobilized enzyme, optimum NaCl concentration was 0.15 M, while the optimum pH remained at 9.0. (C) 2003 Elsevier Ltd. All fights reserved.en
dc.format.extent333-337-
dc.language.isoeng-
dc.publisherElsevier B.V.-
dc.sourceWeb of Science-
dc.subjectpectinmethylesterasept
dc.subjectacerolapt
dc.subjectactivity optimumpt
dc.subjectpurificationpt
dc.subjectimmobilizationpt
dc.titleGelatin-immobilized pectinmethylesterase for production of low methoxyl pectinen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionInst Super Tecn-
dc.contributor.institutionUniv Lusofona Humanidades & Tecnol-
dc.contributor.institutionBioTrend-
dc.description.affiliationUNESP, Inst Quim, Dept Bioquim & Tecnol Quim, BR-14801970 Araraquara, SP, Brazil-
dc.description.affiliationInst Super Tecn, Ctr Engn Biol & Quim, P-1049001 Lisbon, Portugal-
dc.description.affiliationUniv Lusofona Humanidades & Tecnol, P-1749024 Lisbon, Portugal-
dc.description.affiliationBioTrend, P-2675807 Ramada, Portugal-
dc.description.affiliationFac Ciências & Letras Araraquara Rodovia A, BR-14800501 Araraquara, SP, Brazil-
dc.description.affiliationUnespUNESP, Inst Quim, Dept Bioquim & Tecnol Quim, BR-14801970 Araraquara, SP, Brazil-
dc.identifier.doi10.1016/j.foodchem.2003.09.040-
dc.identifier.wosWOS:000220772800003-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofFood Chemistry-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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