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Intensification of surfactant synthesis in Rhodococcus erythropolis EK-1 cultivated on hexadecane

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Abstract

Activity of key enzymes of n-alkane metabolism was determined in cells of Rhodococcus erythropolis EK-1, a surfactant producer grown on n-hexadecane. Potassium cations were found to inhibit alkane hydroxylase and NADP+-dependent aldehyde dehydrogenase, while sodium cations were found to activate these enzymes. Decreased potassium concentration (to 1 mM), increased sodium concentration (to 35 mM), and addition of 36 μmol/l Fe(II), required for alkane hydroxylase activity, resulted in increased activity of the enzymes of n-hexadecane metabolism and in a fourfold increase of surfactant synthesis. A 1.5–1.7-fold increase in surfactant concentration after addition of 0.2% fumarate (gluconeogenesis precursor) and 0.1% citrate (lipid synthesis regulator) to the medium with n-hexadecane results from enhanced synthesis of trehalose mycolates, as evidenced by a 3–5-fold increase in phosphoenolpyruvate synthetase and trehalose phosphate synthase, respectively.

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Abbreviations

AlkB:

alkane hydroxylase

NDMA:

4-nitroso-N,N-dimethylaniline

PQQ:

pyrrole quinoline quinone

UDP:

uridine diphosphate

PEP:

phosphoenolpyruvate

TCA:

cycle-tricarboxylic acid cycle

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Authors and Affiliations

  1. Institute of Microbiology and Virology, National Academy of Sciences of Ukraine, Kiev, 03680, Ukraine

    T. P. Pirog, T. A. Shevchuk & Yu. A. Klimenko

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  1. T. P. Pirog
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  2. T. A. Shevchuk
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  3. Yu. A. Klimenko
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Correspondence to T. P. Pirog.

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Original Russian Text © T.P. Pirog, T.A. Shevchuk, Yu.A. Klimenko, 2010, published in Prikladnaya Biokhimiya i Mikrobiologiya, 2010, Vol. 46, No. 6, pp. 651–658.

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Pirog, T.P., Shevchuk, T.A. & Klimenko, Y.A. Intensification of surfactant synthesis in Rhodococcus erythropolis EK-1 cultivated on hexadecane. Appl Biochem Microbiol 46, 599–606 (2010). https://doi.org/10.1134/S0003683810060074

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