Debaryomyces hansenii UFV-1 intracellular α-Galactosidase characterization and comparative studies with the extracellular enzyme

dc.creatorRezende, Sebastião T. de
dc.creatorViana, Pollyanna A.
dc.creatorPassos, Flávia Maria Lopes
dc.creatorOliveira, Jamil S.
dc.creatorTeixeira, Kádima N.
dc.creatorSantos, Alexandre M. C.
dc.creatorBemquerer, Marcelo P.
dc.creatorRosa, José C.
dc.creatorSantoro, Marcelo M.
dc.creatorGuimarães, Valéria M.
dc.date2018-05-29T10:24:11Z
dc.date2018-05-29T10:24:11Z
dc.date2009-02-18
dc.date.accessioned2023-09-27T21:00:44Z
dc.date.available2023-09-27T21:00:44Z
dc.identifierhttp://dx.doi.org/10.1021/jf8030919
dc.identifier15205118
dc.identifierhttp://www.locus.ufv.br/handle/123456789/19852
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8952791
dc.descriptionDebaryomyces hansenii cells cultivated on galactose produced extracellular and intracellular α-galactosidases, which showed 54.5 and 54.8 kDa molecular mass (MALDI-TOF), 60 and 61 kDa (SDS−PAGE) and 5.15 and 4.15 pI values, respectively. The extracellular and intracellular deglycosylated forms presented 36 and 40 kDa molecular mass, with 40 and 34% carbohydrate content, respectively. The N-terminal sequences of the α-galactosidases were identical. Intracellular α-galactosidase showed smaller thermostability when compared to the extracellular enzyme. D. hansenii UFV-1 extracellular α-galactosidase presented higher kcat than the intracellular enzyme (7.16 vs 3.29 s^−1, respectively) for the p-nitrophenyl-α-d-galactopyranoside substrate. The Km for hydrolysis of pNPαGal, melibiose, stachyose, and raffinose were 0.32, 2.12, 10.8, and 32.8 mM, respectively. The intracellular enzyme was acompetitively inhibited by galactose (Ki = 0.70 mM), and it was inactivated by Cu(II) and Ag(I). Enzyme incubation with soy milk for 6 h at 55 °C reduced stachyose and raffinose amounts by 100 and 73%, respectively.
dc.formatpdf
dc.formatapplication/pdf
dc.languageeng
dc.publisherJournal of Agricultural and Food Chemistry
dc.relationv. 57, n. 06, p. 2515–2522, Fevereiro 2009
dc.rightsAmerican Chemical Society
dc.subjectCharacterization
dc.subjectDebaryomyces hansenii UFV-1
dc.subjectDeglycosylation
dc.subjectGalacto-oligosaccharides
dc.subjectα-Galactosidases
dc.titleDebaryomyces hansenii UFV-1 intracellular α-Galactosidase characterization and comparative studies with the extracellular enzyme
dc.typeArtigo


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