dc.creatorBuurman, Ed T.
dc.creatorBoiardi, José Luis
dc.creatorTeixeira de Mattos, M. Joost
dc.creatorNeijssel, Oense M.
dc.date1990
dc.date2022-06-29T15:18:52Z
dc.date.accessioned2023-07-15T04:47:40Z
dc.date.available2023-07-15T04:47:40Z
dc.identifierhttp://sedici.unlp.edu.ar/handle/10915/138545
dc.identifierissn:0302-8933
dc.identifierissn:1432-072X
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/7470910
dc.descriptionMagnesium-limited chemostat cultures of Klebsiella pneumoniae NCTC 418 with 20 μM CaCl2 in the medium showed a low rate of gluconate plus 2-ketogluconate production relative to potassium- or phosphate-limited cultures. However, when the medium concentration of CaCl2 was increased to 1 mM, the glucose dehydrogenase (GDH) activities also increased and became similar to those observed in potassium- or phosphate limited cultures. It is concluded that this is due to Mg2+ and Ca2+ ions being involved in the binding of pyrroloquinoline quinone (PQQ) to the GDH apoenzyme. There seems to be an absolute requirement of divalent cations for proper enzyme functioning and in this respect Ca2+ ions could replace Mg2+ ions. The high GDH activity which has been found in cells grown under Mg2−-limited conditions in the presence of higher concentrations of Ca2+ ions, is compatible with the earlier proposal that GDH functions as an auxiliary energy generating system involved in the maintenance of high transmembrane ion gradients.
dc.descriptionCentro de Investigación y Desarrollo en Fermentaciones Industriales
dc.formatapplication/pdf
dc.format502-505
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-sa/4.0/
dc.rightsCreative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.subjectQuímica
dc.subjectKlebsiella pneumoniae
dc.subjectChemostat culture
dc.subjectGlucose metabolism
dc.subjectGlucose dehydrogenase
dc.subjectPyrroloquinoline quinone
dc.subjectMagnesium
dc.subjectCalcium
dc.titleThe role of magnesium and calcium ions in the glucose dehydrogenase activity of <i>Klebsiella pneumoniae</i> NCTC 418
dc.typeArticulo
dc.typeArticulo


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