Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/66562
Full metadata record
DC FieldValueLanguage
dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleExtraction and partial characterization of peroxidase from Copaifera langsdorffii Desf. leavespt_BR
dc.contributor.authorMaciel, HPFpt_BR
dc.contributor.authorGouvea, CMCPpt_BR
dc.contributor.authorPastore, GMpt_BR
unicamp.author.emailcibelegouvea@hotmail.compt_BR
unicamp.authorCagdo Paiva Gouvea, Cibele Marli Univ Fed Alfenas, Dept Ciencias Biol, BR-37130000 Alfenas, MG, Brazilpt_BR
unicamp.authorFreire Maciel, Hermelinda Penha Pastore, Glaucia Maria Univ Estadual Campinas, Dept Ciencia Alimentos, Fac Engn ALimentos, Campinas, SP, Brazilpt_BR
dc.subjectcopaibapt_BR
dc.subjectenzymept_BR
dc.subjectvegetal extractpt_BR
dc.subject.wosAscorbate Peroxidasept_BR
dc.subject.wosLipid-peroxidationpt_BR
dc.subject.wosCrude Extractpt_BR
dc.subject.wosPurificationpt_BR
dc.subject.wosIsoperoxidasespt_BR
dc.subject.wosHydroquinonept_BR
dc.subject.wosAntioxidantspt_BR
dc.subject.wosTissuept_BR
dc.subject.wosFruitspt_BR
dc.description.abstractIn the literature, several processes have been described to obtain peroxidases. The purpose of this work was to obtain peroxidase from Copaifera langsdorffii leaves and characterize it partially using a factorial design of experiments and univaried tests, to confirm the results obtained by the factorial design of experiments. Peroxidase activity was measured using the guaiacol: hydrogen peroxide system. The isolated peroxidase presented 81.6% of horseradish peroxidase activity and was easy to obtain from leaves of an abundant tree distributed all over the country. Semi-purified peroxidase (COP) was precipitated with acetone 65% (v.v(-1)) of the crude extract, obtaining the acetone powder. The COP optimum reaction pH values were between 5.0-7.0 and the temperatures between 5 and 45 degrees C, with a maximum activity at pH 6.0 and 35 degrees C. The enzyme was stable in temperatures below 50 degrees C and pH from 4.5 to 9.0 for up to 24 hours. The peroxidase was inactivated after 4 hours at 80 degrees C and after 3 minutes at 96 degrees C. This enzyme can possibly be used as a diagnostic reagent, biosensor and for other analytical methods in several fields of Sciences.pt
dc.relation.ispartofCiencia E Tecnologia De Alimentospt_BR
dc.relation.ispartofabbreviationCiencia Tecnol. Aliment.pt_BR
dc.publisher.cityCampinaspt_BR
dc.publisher.countryBrasilpt_BR
dc.publisherSoc Brasileira Ciencia Tecnologia Alimentospt_BR
dc.date.issued2007pt_BR
dc.date.monthofcirculationAPR-JUNpt_BR
dc.identifier.citationCiencia E Tecnologia De Alimentos. Soc Brasileira Ciencia Tecnologia Alimentos, v. 27, n. 2, n. 221, n. 225, 2007.pt_BR
dc.language.isoptpt_BR
dc.description.volume27pt_BR
dc.description.issuenumber2pt_BR
dc.description.firstpage221pt_BR
dc.description.lastpage225pt_BR
dc.rightsabertopt_BR
dc.sourceWeb of Sciencept_BR
dc.identifier.issn0101-2061pt_BR
dc.identifier.wosidWOS:000254832500002pt_BR
dc.identifier.doi10.1590/S0101-20612007000200002pt_BR
dc.date.available2014-11-13T22:37:16Z
dc.date.available2015-11-26T16:02:52Z-
dc.date.accessioned2014-11-13T22:37:16Z
dc.date.accessioned2015-11-26T16:02:52Z-
dc.description.provenanceMade available in DSpace on 2014-11-13T22:37:16Z (GMT). No. of bitstreams: 1 WOS000254832500002.pdf: 152837 bytes, checksum: 296a897b9cb12a956764fd144ec82ee8 (MD5) Previous issue date: 2007en
dc.description.provenanceMade available in DSpace on 2015-11-26T16:02:52Z (GMT). No. of bitstreams: 2 WOS000254832500002.pdf: 152837 bytes, checksum: 296a897b9cb12a956764fd144ec82ee8 (MD5) WOS000254832500002.pdf.txt: 25078 bytes, checksum: 013cf9e3aaf57d0d01e52b323e39503d (MD5) Previous issue date: 2007en
dc.identifier.urihttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/66562pt_BR
dc.identifier.urihttp://www.repositorio.unicamp.br/handle/REPOSIP/66562
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/66562-
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File Description SizeFormat 
WOS000254832500002.pdf149.25 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.