Serine-enriched minimal medium enhances conversion of selenium into selenocysteine by Streptococcus thermophilus
2019
Castañeda-Ovando, A. | Segovia-Cruz, J.A. | Flores-Aguilar, J.F. | Rodríguez-Serrano, G.M. | Salazar-Pereda, V. | Ramírez-Godínez, J. | Contreras-López, E. | Jaimez-Ordaz, J. | González-Olivares, L.G.
Selenium is included in selenoprotein sequences, which participate in enzymatic processes necessary to preserve optimal health. Some lactic acid bacteria carry out the biotransformation of inorganic selenium in their metabolism. The complete biochemical mechanism of selenium biotransformation is still unknown; however, it is known that both the selenocysteine synthesis process and its subsequent incorporation into selenoproteins include serine as part of the action of seryl-RNAt synthetase. Therefore, the aim of this work was to determine the effect of serine during the biotransformation of selenium and the subsequence growth of Streptococcus thermophilus in a minimal medium. Two culture media were prepared, one enriched with the minimum inhibitory concentration of selenite (as Na2SeO3) and the other as a mixture of the minimum inhibitory concentration of selenite and serine. The absorbed selenium concentration was measured by inductively coupled plasma, and the selenocysteine identification was performed by reverse-phase HPLC. In the second culture medium, decreases in both times, the adaptation and the logarithmic phase, were observed. According to the results, it was possible to establish that the presence of serine allowed the biotransformation of selenite into selenocysteine by Strep. thermophilus.
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