Purification and characterization of pectin methylesterase from acerola (Malpighia glabra L.)

dc.contributor.authorde Assis, Sandra Aparecida
dc.contributor.authorMartins, Antonio Baldo Geraldo
dc.contributor.authorde Faria Oliveira, Olga Maria Mascarenhas
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniv Estadual Feira de Santana
dc.date.accessioned2014-05-20T15:28:46Z
dc.date.available2014-05-20T15:28:46Z
dc.date.issued2007-08-15
dc.description.abstractThe enzyme pectinmethylesterase (PME) from acerola was extracted and purified by gel anion-exchange chromatography (Q Sepharose) and filtration on Sephadex G-100. The results showed two different PME isoforms (PME1 and PME2), with molecular masses of 25.10 and 5.20 kDa, respectively. PMEI specific activity increased by 9.63% after 60 min incubation at 98 degrees C, while PME2 retained 66% of its specific activity under the same conditions. The K-m values of PMEI, PME2 and concentrated PME were 0.94, 0.08 and 0.08mg mL(-1), respectively. The V-max value of PMEI, PME2 and concentrated were 204.08, 2, 158.73 and 2.92 mu mol min(-1) mg(-1) protein, respectively. (c) 2007 Society of Chemical Industry.en
dc.description.affiliationUNESP, Dept Bioquim & Tecnol Quim, Inst Quim, BR-14801970 Araraquara, SP, Brazil
dc.description.affiliationUniv Estadual Feira de Santana, Dept Saude, BR-44031460 Feira de Santana, BA, Brazil
dc.description.affiliationUNESP, Dept Hort, Jaboticabal, SP, Brazil
dc.description.affiliationUnespUNESP, Dept Bioquim & Tecnol Quim, Inst Quim, BR-14801970 Araraquara, SP, Brazil
dc.description.affiliationUnespUNESP, Dept Hort, Jaboticabal, SP, Brazil
dc.format.extent1845-1849
dc.identifierhttp://dx.doi.org/10.1002/jsfa.2884
dc.identifier.citationJournal of the Science of Food and Agriculture. Chichester: John Wiley & Sons Ltd, v. 87, n. 10, p. 1845-1849, 2007.
dc.identifier.doi10.1002/jsfa.2884
dc.identifier.issn0022-5142
dc.identifier.urihttp://hdl.handle.net/11449/38525
dc.identifier.wosWOS:000248240800008
dc.language.isoeng
dc.publisherWiley-Blackwell
dc.relation.ispartofJournal of the Science of Food and Agriculture
dc.relation.ispartofjcr2.379
dc.relation.ispartofsjr0,822
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectpectinmethylesterasept
dc.subjectacerolapt
dc.subjectkinetic characterizationpt
dc.subjectpurificationpt
dc.subjectisoenzymespt
dc.subjectheat stabilitypt
dc.titlePurification and characterization of pectin methylesterase from acerola (Malpighia glabra L.)en
dc.typeArtigo
dcterms.licensehttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dcterms.rightsHolderWiley-Blackwell
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Química, Araraquarapt

Arquivos

Licença do Pacote
Agora exibindo 1 - 1 de 1
Nenhuma Miniatura disponível
Nome:
license.txt
Tamanho:
1.71 KB
Formato:
Item-specific license agreed upon to submission
Descrição: