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Revista Latinoamericana de Microbiología

2009, Number 1-2

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Microbiología 2009; 51 (1-2)

Malate dehydrogenase of saccharopolyspora erythraea CA340: Purification and effect of carbon source on its synthesis

Mendoza P, Servín-González L, Flores ME

Language: English
References: 19
Page: 18-22
PDF size: 230.28 Kb.


ABSTRACT

Malate dehydrogenase (MDH) was purified to homogeneity from cell-free extracts of Saccharopolyspora erythraea, an erythromycin producer, and found to be a dimer with an apparent monomer mass of 40 kDa. The enzyme catalyzed preferentially the reduction of oxaloacetic acid with NADH; Km values for oxaloacetate and NADH were 0.015 mM and 0.056 mM, respectively. S. erythraea grown in minimal medium with either glucose, galactose or lactose as carbon sources showed similar levels of MDH specific activity, which were not affected by the growth phase. On the other hand, growth on fructose as carbon source resulted in elevated levels of MDH specific activity that were two-fold higher than in the other carbon sources.


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