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Stimulation of Erwinia sp. Fumarase and aspartase synthesis by changing medium components

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Abstract

The optimal concentrations of nutrient medium components, aeration conditions, and pH providing for maximum biomass yields, as well as fumarase and l-aspartase activities, during submerged cultivation of Erwinia sp. were determined. The data showed that different concentrations of carbon source (molasses) and pH of the nutrient medium were required to reach the maximum fumarase and l-aspartase activities. Calculations performed by application of the additive lattice model suggested that the combination of these optimized factors would result in 3.2-, 3.4-, and 3.8-fold increases as compared to the experimental means in Erwinia sp. biomass, and l-aspartase and fumarase activities, respectively. The conditions of the fumaric acid biotransformations into l-malic and l-aspartic acids were optimized on the basis of intact Erwinia sp. cells, a fumarase and l-aspartase producer. In the cases of fumarate transformation into l-malic acid and of fumarate transformation into l-aspartic acids, fumarase and l-aspartase activities increased 1.5- and 1.7-fold, respectively. The experimental data were consistent with these estimates to 80% accuracy. In comparison with the additive lattice model, the application of polynomial nonlinear model allowed the between-factor relations to be considered and analyzed, which resulted in 1.1-, 1.27-, and 1.1-fold increases in Erwinia sp. biomass and fumarase and l-aspartase activities for the case of cultivation. In the case of fumarate transformation into l-malic acid, this model demonstrated a 1.7-fold increase in fumarase activity, whereas during fumarate transformation into l-aspartic acid no significant change in aspartase activity was observed.

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Correspondence to J. C. Roseiro.

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Bagdasaryan, Z.N., Aleksanyan, G.A., Mirzoyan, A.M. et al. Stimulation of Erwinia sp. Fumarase and aspartase synthesis by changing medium components. Appl Biochem Biotechnol 125, 113–126 (2005). https://doi.org/10.1385/ABAB:125:2:113

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  • DOI: https://doi.org/10.1385/ABAB:125:2:113

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