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dc.contributor.authorDo Amaral, S. H.-
dc.contributor.authorDe Assis, S. A.-
dc.contributor.authorOliveira, OMMD-
dc.identifier.citationJournal of Food Biochemistry. Oxford: Blackwell Publishing, v. 29, n. 4, p. 367-380, 2005.-
dc.description.abstractThe enzyme pectin methylesterase (PME) from orange was extracted and partially purified by filtration on Sephadex G-100. The extraction buffer for orange PME was borate-acetate containing 0.4 M NaCl. Orange PME showed optimum pH at 8.0 and optimum temperature at 50C. The PME enzyme was completely inactivated after 1 min of incubation at 90C. The specific activity increased in the presence of 0.15 M NaCl or 0.025 M Na2SO4, 0.10 M KCl, 0.025 M K2SO4, 0.05 and 0.1 M NH4Cl. Lithium chloride and Li(2)SO(4)inhibited the enzymatic activity at all concentrations studied. The K-m and V(max)value of PME were 0.36 mg/mL and 5.26 mu mol/mL-mg protein, respectively.en
dc.publisherBlackwell Publishing-
dc.sourceWeb of Science-
dc.titlePartial purification and characterization of pectin methylesterase from orange (Citrus sinensis) cv. Pera-rioen
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniv Estadual Feira Santana-
dc.description.affiliationUNESP, Inst Quim, Dept Bioquim & Tecnol Quim, BR-14801970 Araraquara, SP, Brazil-
dc.description.affiliationUniv Estadual Feira Santana, Dept Saude, BR-44031460 Feira de Santana, BA, Brazil-
dc.description.affiliationUnespUNESP, Inst Quim, Dept Bioquim & Tecnol Quim, BR-14801970 Araraquara, SP, Brazil-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofJournal of Food Biochemistry-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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