Enhanced Production of Benzoylformate Reductase in Enterococcus faecalis under Oxidative Stress Established by Natural Electron Carriers

  • Baik, Sang-Ho (Marine Biotechnology Institute, Kamaishi City) ;
  • Cho, Pan-Ki (Doosan R&D Center) ;
  • Kim, Mee-Hae (Department of Food Science and Technology and Institute of Agricultural Science and Technology, Chonbuk National University) ;
  • Yun, Sei-Eok (Department of Food Science and Technology and Institute of Agricultural Science and Technology, Chonbuk National University)
  • Published : 2003.02.01

Abstract

Enhancement of the production of benzoylformate reductase (BFR) was attempted under oxidative stress established by natural electron carriers. -lipoic acid (LA), flavin adenine dinucleotide (FAD), and ubiquinone (UQ) did not inhibit growth of E. faecalis when their concentrations were as high as $10{\mu}M$, while $H_2O_2$ and methyl viologen ($MV^2+$) inhibited the bacterial growth. BFR activity in the bacterial extract had increased rapidly after 1 h of cultivation after the addition of $4{\mu}M$ of natural electron carriers, and the activity was maintained during further cultivation. BFR activity of the cells treated with the natural electron carriers was $40\%$ higher than that of the control. In the presence of $4{\mu}M\;H_2O_2\;and\;MV^2+$, BFR activity increased, reaching the highest activity at about 5 h cultivation, and then decreased with further cultivation. It seems that natural electron carriers not only stimulate the induction of BFR, but also stabilize the enzyme. BFR was hardly affected by LA, FAD, and UQ, while $H_2O_2\;and\;MV^2+$ inactivated the crude enzyme. The decrease of BFR activity in the presence of $H_2O_2\;and\;MV^2+$ might be ascribed to inactivation of the enzyme by the oxidants.

Keywords

References

  1. J. Microbiol. Biotechnol. v.11 Physiological responses of oxygen-tolerant anaerobic Bifidobacterium longum under oxygen Ahn J. B.;H. J. Hwang;J. H. Park
  2. Cell v.47 Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium Christman M. F.;R. W. Morgan;F. S. Jacobson;B. N. Ames
  3. Annu. Rev. Genet. v.25 regulation of bacterial oxidative stress genes Demple B. https://doi.org/10.1146/annurev.ge.25.120191.001531
  4. Nature v.304 Inducible repair of oxidative DNA damage in Escherichia coli Demple B.;J. Halbrook https://doi.org/10.1038/304466a0
  5. Microb. Rev. v.55 Oxidative stress responses in Escherichia coli and Salmonella typhimurium Farr S. B.;T. Kogoma
  6. Die Praxis des Organischen Chemiker(2nd ed.) Gattermann L.;H. Wieland
  7. J. Bacteriol. v.171 A global response induced in Escherichia coli by redox-cycling agents overlaps with that induced by peroxide stress Greenberg J. T.;B. Demple
  8. J. Biotechnol. v.14 Construction of a bioreactor for production of (R)-(-)-mandelate, a typical specialty chemical Hosono K.;S. Kajiwara;Y. Yamazaki;H. Maeda https://doi.org/10.1016/0168-1656(90)90003-T
  9. J. Biosci. Bioeng. v.90 Utilization of oxidative pressure for enhanced production of poly-${\beta}$-hydroxybutyrate and poly (3-hydroxybutyrate-3-hydroxyvalerate) in Ralstonia eutropha Jung Y. M.;Y. H. Lee
  10. J. Biol. Chem. v.260 Biochemical characterization of a paraquat-tolerant mutant of Escherichia coli. Koa S. M.;H. M. Hassan
  11. J. Microbiol. Biotechnol. v.10 Stress responses of the Escherichia coli groE promoter Kwak Y. H.;S. J. Kim;K. Y. Lee;H. B. Kim
  12. J. Microbiol. Biotechnol. v.12 Effect of dissolved oxygen concentration and pH on the mass production of high molecular weight pullulan by Aureobasidium pullulans Lee J. H.;J. H. Kim;M. R. Kim;S. M. Lim;S. W. Nam;J. W. Lee;S. K. Kim
  13. Molec. Microbiol. v.5 The molecular basis of carbon-starvation induced general resistance in Escherichia coli. Martin A. https://doi.org/10.1111/j.1365-2958.1991.tb01819.x
  14. Tetrahedron v.36 Synthesis of optically active alkenyl alcohols and ${\alpha}$-hydroxy esters by microbial asymmetric hydrolysis by the corresponding acetates Mori K.;H. Akao https://doi.org/10.1016/0040-4020(80)85030-7
  15. J. Org. Chem. v.46 Enzymatic conversion of ${\alpha}$-keto aldehydes to optically active ${\alpha}$-hydroxy acids using glyoxalase I and II Patterson M. A. K.;R. P. Szajewski;G. M. Whitesides https://doi.org/10.1021/jo00336a011
  16. J. Virol v.68 Heat shock response to vaccinia virus infection Sedger L.;J. Ruby
  17. Methods in Enzymology v.236 Regulation of bacterial gene expression in response to oxidative stress Storz G.;M. B. Toledano;V. L. Clark (ed.);P. M. bavoil (ed.) https://doi.org/10.1016/0076-6879(94)36017-0
  18. Free Radical Biol. v.22 Oxidants as stimulators of signal transduction Suzuki Y. J.;H. J. Forman;A. Sevanian https://doi.org/10.1016/S0891-5849(96)00275-4
  19. Res. Microbiol. v.152 Hydrogen peroxide effects on Streptococcus thermophilus CNRZ 368 cell viability Thibessard A.;A. Fernandez;B. Gintz;N. Leblond Bourget;B. Decaris https://doi.org/10.1016/S0923-2508(01)01234-7
  20. J. Bacteriol v.172 SoxR, a locus governing a superoxide response regulon in Escherichia coli K-12 Tsaneva I. R.;B. Beiss
  21. Appl. Environ. Microbiol. v.177 Synergistic induction of the heat shock response in Escherichia coli by simultaneous treatment with chemical inducers van Dyk T. K.;T. R. Reed;A. C. Vollmer;R. A. LaRossa
  22. Agric. Biol. Chem. v.50 Enzymatic synthesis of optically pure (R)-(-)-mandelic acid and other 2-hydroxycarboxylic acids: Screening for the enzyme and its purification, characterization and use Yamazaki Y.;H. Maeda https://doi.org/10.1271/bbb1961.50.2621