Applied Microbiology and Biotechnology

, Volume 32, Issue 4, pp 455–460 | Cite as

The production of molecular hydrogen byEscherichia coli during ampicillin-induced spheroplast formation

  • E. G. Hörnsten
  • L. E. Nilsson
  • B. Danielsson
Article
Received:
Accepted:

Summary

The present study examined the effects of ampicillin-induced spheroplast formation on the production of molecular hydrogen byEscherichia coli carrying out fermentation in a lactosepeptone broth with an osmolality of 342 mosmol/l. The effects were most pronounced during the transformation of bacterial cells to spheroplasts. It was shown that the lower production rate of molecular hydrogen by spheroplastic cells is due not only to a suggested decrease in mixed-acid fermentation but also to a reduction in hydrogenlyase activity.

Keywords

Hydrogen Fermentation Production Rate Bacterial Cell Lower Production 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
This is a preview of subscription content, log in to check access.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Ånséhn S, Nilsson L (1984) Direct membrane-damaging effect of ketoconazole and tioconazole onCandida albicans demonstrated by bioluminescent assay of ATP. Antimicrob Agents Chemother 26:22–25Google Scholar
  2. Ballantine SP, Boxer DH (1986) Isolation and characterization of a soluble fragment of hydrogenase isoenzyme 2 from the membranes of anaerobically grownEscherichia coli. Eur J Biochem 156:277–84Google Scholar
  3. Cole JA, Wimpenny JWT (1966) The inter-relationships of low redox potential cytochrome C552 and hydrogenase in facultative anaerobes. Biochim Biophys Acta 128:419–25Google Scholar
  4. Cronan JE Jr, Gennis RB, Maloy SR (1987) Cytoplasmic membrane. In: Neidhardt FC (ed)Escherichia coli andSalmonella typhimurium. American Society for Microbiology, Washington, DC, USA, vol 1. pp 31–35Google Scholar
  5. Danielsson B, Mosbach K (1988) Enzyme thermistors. Methods Enzymol 137:181–197Google Scholar
  6. Gnarpe H (1970) Spheroplast infections in the urinary tract. Scand J Infect Dis 2:59–64Google Scholar
  7. Harden A (1901) The chemical action ofBacillus coli communis and similar organisms on carbohydrates and allied compounds. J Chem Soc 79:601–28Google Scholar
  8. Hörnsten EG, Elwing H, Kihlström E, Lundström I (1985) Sensorized determination of molecular hydrogen in investigations of the susceptibility of Enterobacteriaceae to ampicillin. J Antimicrob Chemother 15:695–700Google Scholar
  9. Hörnsten EG, Daniellson B, Elwing H, Lundström I (1986) Sensorized on-line determinations of molecular hydrogen inEscherichia coli fermentations. Appl Microbiol Biotechnol 24:117–121Google Scholar
  10. Hörnsten EG, Lunström I, Elwing H (1989a) Some biometrical applications of molecular hydrogen and ammonia determinations by the use of metal-oxide-semiconductor devices. In: Wise DL (ed) Bioinstrumentation: research, developments and applications. Butterworth, Boston, pp 47–91Google Scholar
  11. Hörnsten EG, Nilsson LE, Elwing H, Lundström I (1989b) Effects ofEscherichia coli spheroplast formation on assays of H2 and adenosine triphosphate-based ampicillin susceptibility tests. Diagn Microbiol Infect Dis 12:171–175Google Scholar
  12. Ingraham J (1987) Effect of temperature, pH, water activity and pressure on growth. In: Neidhardt FC (ed)Escherichia coli andSalmonella typhimurium. American Society for Microbiology, Washington, DC, USA, vol 2. pp 1543–54Google Scholar
  13. Lundin A (1982) Analytical applications of bioluminescence: the firefly system. In: Kricka L (ed) Clinical and biochemical luminescence. Marcel Dekker, New York, pp 43–74Google Scholar
  14. Lundström I (1981) Hydrogen sensitive MOS-structures, Part 1; principles and applications. Sensors Actuators 1:403–426Google Scholar
  15. Maloney PC (1987) Coupling to an energized membrane: role of ion-motive gradients in the transduction of metabolic energy. In: Neidhardt FC (ed)Escherichia coli andSalmonella typhimurium. American Society for Microbiology, Washington DC, USA, vol. 1. pp 222–43Google Scholar
  16. Melchior NH, Blom J, Tybring L, Birch-Andersen A (1973) Light and electron microscopy of the early response ofEscherichia coli to 6β-amidinopenicillanic acid (FL 1060). Acta Pathol Microbiol Scand [B] 81:393–407Google Scholar
  17. Motteram PAS, McCarthy JEG, Ferguson SJ, Jackson JB, Cole JA (1981) Energy conservation during the formate dependent reduction of nitrite byEscherichia coli. FEMS Microbiol Lett 12:317–20Google Scholar
  18. Nilsson L (1978) New rapid bioassay of gentamicin based on luciferase assay of extracellular ATP in bacterial cultures. Antimicrob Agents Chemother 14:812–16Google Scholar
  19. Pakes WCC, Jollyman WH (1901) The bacterial decomposition of formic acid into carbon dioxide and hydrogen. J Chem Soc 79:386–91Google Scholar
  20. Sawers RG, Boxer DH (1986) Purification and properties of membrane-bound hydrogenase isoenzyme 1 from anaerobically grownEscherichia coli K12. Eur J Biochem 156:265–75Google Scholar
  21. Sawers RG, Ballantine SP, Boxer DH (1985) Differential expression of hydrogenase isoenzymes inEscherichia coli K12: evidence for a third isoenzyme. J Bacteriol 164:1324–31Google Scholar
  22. Thrupp LD (1986) Susceptibility testing of antibiotics in liquid media. In: Lorian V (ed) Antibiotics in laboratory medicine. Williams and Wilkins, Baltimore, pp 93–150Google Scholar
  23. Wu LF, Mandrand-Berthelot MA (1986) Genetic and physiological characterization of newEscherichia coli mutants impaired in hydrogenase activity. Biochimie 68:167–79Google Scholar

Copyright information

© Springer-Verlag 1990

Authors and Affiliations

  • E. G. Hörnsten
    • 1
  • L. E. Nilsson
    • 2
  • B. Danielsson
    • 3
  1. 1.Biology group of the Laboratory of Applied PhysicsLinköping Institute of TechnologyLinköpingSweden
  2. 2.Department of Clinical BacteriologyLinköping University HospitalLinköpingSweden
  3. 3.Department of Applied BiochemistryUniversity of LundLundSweden

Personalised recommendations