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


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Article Info

DATE

2010-11

AUTHORS

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

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. More... »

PAGES

599-606

References to SciGraph publications

  • 2007-02. Alkane hydroxylases involved in microbial alkane degradation in APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • 2007-10. Bacterial metabolism of long-chain n-alkanes in APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • 2005-09. A novel nicotinoprotein aldehyde dehydrogenase involved in polyethylene glycol degradation in APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • Identifiers

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    http://scigraph.springernature.com/pub.10.1134/s0003683810060074

    DOI

    http://dx.doi.org/10.1134/s0003683810060074

    DIMENSIONS

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