1887

Abstract

and 18 representative strains of the genus were examined for the presence of NAD-dependent dehydrogenases for lactate, ethanol or 2,3-butanediol after the cells had been transiently cultivated under conditions of oxygen deficiency. Formation of these enzymes was derepressed in all strains except and . The protein patterns of and type strain and strains N9A, H16, B19, H1 and H20 obtained by PAGE were similar. The purified lactate dehydrogenases from these strains were strongly inhibited by 1 to 5 μ-oxaloacetate, had a broad substrate specificity and a high affinity for Matrex Gel Green A. shared the properties of the lactate dehydrogenase but differed greatly with respect to its protein pattern. In strain A7 a high activity of lactate dehydrogenase was detected, but the enzyme was not sensitive to oxaloacetate.

Alcohol dehydrogenase and 2,3-butanediol dehydrogenase were even more widely distributed than lactate dehydrogenase among the strains studied. In many cases the electrophoretic mobilities of both alcohol dehydrogenases were identical. The study results in the following taxonomical conclusions. type strain and strains N9A, H16, B19, H1 and H20 are almost identical with respect to protein and enzyme patterns as well as the presence of a derepressible L(+)-lactate dehydrogenase sensitive to oxaloacetate. The strains CH34, 707, A7 and JMP134 differ greatly from this core group and from each other and have to be considered as aberrant strains of .

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-129-9-2825
1983-09-01
2021-08-04
Loading full text...

Full text loading...

/deliver/fulltext/micro/129/9/mic-129-9-2825.html?itemId=/content/journal/micro/10.1099/00221287-129-9-2825&mimeType=html&fmt=ahah

References

  1. Atkinson T., Hammond P.M., Hartwell R.D., Hughes P, Scawen M.D., Sherwood R.F., Small D.A.P., Bruton C.J., Harvey M.J., Lowe C.R. 1981; Triazine-dye affinity chromatography. Biochemical Society Transactions 9:290–293
    [Google Scholar]
  2. Bergmeyer H.U. 1974 Methoden der Enzymatis-chen Analyse 1, 3rd edn.. Weinheim: Verlag Chemie:
    [Google Scholar]
  3. Beudeker R.F., De Boer W., Kuenen J.G. 1981; Heterolactic fermentation of intracellular polyglucose by the obligate chemolithotroph Thiobacillus neapolitanus under anaerobic conditions. FEMS Microbiology Letters 12:337–342
    [Google Scholar]
  4. Bradford M.M. 1976; A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Analytical Biochemistry 72:248–254
    [Google Scholar]
  5. Friedrich B., Hogrefe C., Schlegel H.G. 1981a; Naturally occurring genetic transfer of hydrogen-oxidizing ability between strains of Alcali-genes eutrophus. . Journal of Bacteriology 147:198–205
    [Google Scholar]
  6. Friedrich C.G., Friedrich B., Bowien B. 1981b; Formation of enzymes of autotrophic metabolism during heterotrophic growth of Alcali-genes eutrophus. . Journal of General Microbiology 122:69–78
    [Google Scholar]
  7. Garvie E.L. 1980; Bacterial lactate dehydrogenases. Microbiological Reviews 44:83–105
    [Google Scholar]
  8. Höhn-Bentz H., Radler F. 1978; Bacterial 2,3-butanediol dehydrogenases. Archives of Microbiology 116:197–203
    [Google Scholar]
  9. Jüttner R.R., Lafferty R.M., Knackmuss H.J. 1975; A simple method for the determination of poly-β-hydroxybutyric acid in microbial biomass. European Journal of Applied Microbiology 1:233–237
    [Google Scholar]
  10. Kersters K., De Ley J. 1980; Classification and identification of bacteria by electrophoresis of their proteins. In Microbiological Classification and Identification pp. 273–297 Goodfellow M., Board R.G. Edited by London: Academic Press.;
    [Google Scholar]
  11. Kersters K., Segers P., Gayral J.P., De Ley J. 1981; The taxonomy of the genus Alcaligenesstudied by auxanography and DNA :rRNA hybridizations. In Abstracts of the IV International Conference on Culture Collections p. 34 Brno.
    [Google Scholar]
  12. Mergeay M., Houba C., Gerits J. 1978; Extrachromosomal inheritance controlling resistance to cadmium, cobalt and zinc ions: evidence from curing in a Pseudomonas. . Archives internationales de physiologic et de biochimie 86:440–441
    [Google Scholar]
  13. Nokhal T.-H.A.A. 1981 Paracoccus denitrificans: Neuisolation und Untersuchungen zur Taxonomic und Stoffwechselphysiologie pp. 117–151 Dissertation, Universität Göttingen, F.R.G.:
    [Google Scholar]
  14. Ohi K., Takada N., Komemushi S., Okazaki M., Miura Y. 1979; A new species of hydrogenutilizing bacterium. Journal of General and Applied Microbiology 25:53–58
    [Google Scholar]
  15. Palleroni N.J., Palleroni A.V. 1978; Alcaligenes latus, a new species of hydrogen-utilizing bacteria. International Journal of Systematic Bacteriology 28:416–426
    [Google Scholar]
  16. Pemperton J.M., Corney B., Don R.H. 1979; Evolution and spread of pesticide degrading ability among soil microoganisms. In Plasmids of Medical, Environmental and Commercial Importance pp. 287–299 Timmis K.N., Piihler A. Edited by Amsterdam: Elsevier/North Holland Biomedical Press.;
    [Google Scholar]
  17. Riley M., Anilionis A. 1978; Evolution of the bacterial genome. Annual Review of Microbiology 32:519–560
    [Google Scholar]
  18. Schlegel H.G. 1983; Studies on the regulation and genetics of enzymes of Alcaligenes eutrophus. In Microbial Ecology and Metabolism. Codd G.A., Stewart W.D.P. Edited by London, New York: Academic Press; in the press
    [Google Scholar]
  19. Schlegel H.G., Steinbüchel A. 1981; Die relative Respirationsrate (RRR), ein neuer Belfiftungsparameter. In Fermentation pp. 11–26 Lafferty R.M. Edited by Wien, New York: Springer Verlag;
    [Google Scholar]
  20. Schlegel H.G., Vollbrecht D. 1980; Formation of the dehydrogenases for lactate, ethanol and butanediol in the strictly aerobic bacterium Alcaligenes eutrophus. . Journal of General Microbiology 117:475–481
    [Google Scholar]
  21. Schuster E. 1967 Chemolithotrophes Wachstum von Hydrogenomonas H16 im Chemostaten mit elektroly-tischer Knallgaserzeugung. Dissertation, Universität Göttingen, F.R.G.:
    [Google Scholar]
  22. Schwien U., Schmidt E. 1982; Improved degradation of monochlorophenols by a constructed strain. Applied and Environmental Microbiology 44:33–39
    [Google Scholar]
  23. Senior P.J. 1973; The regulation of poly-β-hydroxybutyrate metabolism in Azotobacter beijerinckii. Biochemical Journal 134:225–238
    [Google Scholar]
  24. Senior P.J., Beech G.A., Ritchie G.F., Dawes E.A. 1972; The role of oxygen limitation in the formation of poly-β-hydroxybutyrate during batch and continuous culture of Azotobacter beijerinckii. Biochemical Journal 128:1193–1201
    [Google Scholar]
  25. Steinbüchel A., Schlegel H.G. 1983a; NAD-linked l(+)-lactate dehydrogenase from the strict aerobe Alcaligenes eutrophus. 1. Purification and properties. European Journal of Biochemistry 130:321–328
    [Google Scholar]
  26. Steinbüchel A., Schlegel H.G. 1983b; NAD-linked l(+)-lactate dehydrogenase from the strict aerobe Alcaligenes eutrophus. 2. Kinetic properties and inhibition by oxaloacetate. European Journal of Biochemistry 130:329–334
    [Google Scholar]
  27. Steinbüchel A., Schlegel H.G. 1983C; The rapid purification of lactate dehydrogenase from Alcaligenes eutrophus in a two-step procedure. European Journal of Applied Microbiology and Biotechnology 17:163–167
    [Google Scholar]
  28. Vollbrecht D. 1980; Oxygen deficiency and excretion of metabolites by strictly aerobic bacteria. Biotechnology Letters 2:49–54
    [Google Scholar]
  29. Vollbrecht D., El Nawawy M.A. 1980; Restricted oxygen supply and excretion of metabolites. I.Pseudomonas spec, and Paracoccus denitrificans. European Journal of Applied Microbiology and Biotechnology 8:135–143
    [Google Scholar]
  30. Weber K., Osborn M. 1969; The reliability of molecular weight determinations by dodecyl sulfate polyacrylamide gel electrophoresis. Journal of Biological Chemistry 244:4406–4412
    [Google Scholar]
  31. Wilde E. 1962; Untersuchungen fiber Wachstum und Speicherstoffsynthese von Hydrogenomonas. Archiv für Mikrobiologie 43:109–137
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-129-9-2825
Loading
/content/journal/micro/10.1099/00221287-129-9-2825
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error