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Utilize este identificador para citar ou criar um link para este item: http://acervodigital.unesp.br/handle/11449/68324
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dc.contributor.authorHiroito Obara, Francis Widmann-
dc.contributor.authorVaréa-Pereira, Geni-
dc.contributor.authorTomoe Miyagui, Dalva-
dc.contributor.authorCorradi Da Silva, Maria de Lourdes-
dc.date.accessioned2014-05-27T11:21:23Z-
dc.date.accessioned2016-10-25T18:20:55Z-
dc.date.available2014-05-27T11:21:23Z-
dc.date.available2016-10-25T18:20:55Z-
dc.date.issued2005-07-01-
dc.identifierhttp://dx.doi.org/10.4025/actascibiolsci.v27i3.1317-
dc.identifier.citationActa Scientiarum - Biological Sciences, v. 27, n. 3, p. 303-310, 2005.-
dc.identifier.issn1679-9283-
dc.identifier.urihttp://hdl.handle.net/11449/68324-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/68324-
dc.description.abstractLaccases are glycoprotein polyphenol oxidases which are involved in fungal pathogenicity and they are also useful for biotechnological applications. The ligninolytic ascomycete, Botryosphaeria rhodina, has been studied as producer of exopolysaccharide and PPO-I and PPO-II laccases induced by veratryl alcohol. However, as the induced laccases have not been isolated, the aim of this study was to purify the enzyme and to identify the carbohydrates constituents of the glycosidic moiety. The fungus was cultivated on broth Vogel, 1% glucose and 30.4mM veratryl alcohol during 4.5 days at 28°C/180 rpm. The extracellular fluid showed high carbohydrate concentration and the stability of PPO-I laccase under conditions of refrigeration and freezing at 4°C-18°C over 40 days. The purification was developed by ultrafiltration using a NMWL 100 and 30 kDa membrane, gelfiltration on Sephadex G-100, and ion-exchange chromatography on DEAE-cellulose. The purified laccase was identified as a glycoprotein, weight molecular 113 kDa, consisting of 40% protein and 60% carbohydrate identified by HPAEC-PAD as fucose, galactose, mannose, glucose and glucosamine.en
dc.format.extent303-310-
dc.language.isopor-
dc.sourceScopus-
dc.subjectBotryosphaeria rhodina-
dc.subjectCharacterization-
dc.subjectExopolysaccharides-
dc.subjectGlycoprotein-
dc.subjectLaccase-
dc.subjectPurification-
dc.subjectexopolysaccharide-
dc.subjectfucose-
dc.subjectgalactose-
dc.subjectglucosamine-
dc.subjectglucose-
dc.subjectglycoprotein-
dc.subjectlaccase-
dc.subjectpolyphenol-
dc.subjectsephadex-
dc.subjectAscomycetes-
dc.subjectbiotechnology-
dc.subjectenzyme isolation-
dc.subjectenzyme purification-
dc.subjectenzyme stability-
dc.subjectextracellular fluid-
dc.subjectfungal virulence-
dc.subjectfungus-
dc.subjectgel filtration-
dc.subjection exchange chromatography-
dc.subjectnonhuman-
dc.subjectultrafiltration-
dc.subjectAscomycota-
dc.subjectFungi-
dc.titlePurificação de lacases PPO-I de Botryosphaeria rhodinapt
dc.title.alternativePurification of laccases PPO-I of fungus Botryosphaeria rhodinaen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual de Londrina (UEL)-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationDepartamento de Bioquímica e Biotecnologia Universidade Estadual de Londrina (UEL) Campus Universitário, Cx. Postal 6001, 86051-990, Londrina, Paraná-
dc.description.affiliationDepartamento de Física, Química e Biologia Faculdade de Ciências e Tecnologia Universidade Estadual Paulista (Unesp), Rua Roberto Simonsen, 305, 19060-900, Presidente Prudente, SP-
dc.description.affiliationUnespDepartamento de Física, Química e Biologia Faculdade de Ciências e Tecnologia Universidade Estadual Paulista (Unesp), Rua Roberto Simonsen, 305, 19060-900, Presidente Prudente, SP-
dc.identifier.doi10.4025/actascibiolsci.v27i3.1317-
dc.rights.accessRightsAcesso aberto-
dc.identifier.file2-s2.0-33645714170.pdf-
dc.relation.ispartofActa Scientiarum: Biological Sciences-
dc.identifier.scopus2-s2.0-33645714170-
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