1887

Abstract

produced one mole of (–)-lactate per mole of glucose used at all dilution rates in ammonia-limited continuous culture. In contrast, lactate production varied according to the dilution rate when glucose was the limiting nutrient. At dilution rates of less than 0·2 h, acetate and propionate were the main fermentation products and lactate production was low. At dilution rates above 0·2 h, the pattern changed to one of high lactate production similar to that under ammonia limitation. Experiments with cell-free extracts of showed that (–)-lactate dehydrogenase had sigmoidal kinetics consistent with homotropic activation of the enzyme by its substrate, pyruvate. This feature allows to amplify the effects of relatively small changes in the intracellular concentration of pyruvate to cause much larger changes in the rate of production of lactate. Some confirmation that this mechanism of control occurs under physiological conditions was obtained in glucose-limited culture, in which the sigmoidal increase in lactate production was accompanied by a linear increase in pyruvate excretion as the dilution rate increased.

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1978-07-01
2021-05-18
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References

  1. Baker K. 1968; Low cost continuous culture apparatus. Laboratory Practice 17:817–824
    [Google Scholar]
  2. Clark B., Holms W. H. 1976; Control of the sequential utilization of glucose and fructose by Escherichia coli . Journal of General Microbiology 95:191–201
    [Google Scholar]
  3. Clark B., Porteous J. W. 1964; Determination of succinic acid by an enzymic method. Biochemical Journal 93:21c
    [Google Scholar]
  4. Conway E. J. 1957; Microdiffusion Analysis and Volumetric Error. , 4.277–278 London: Crosby Lockwood & Son;
    [Google Scholar]
  5. Crow V. L., Pritchard G. G. 1977; Fructose 1,6-diphosphate-activated l-lactate dehydrogenase from Streptococcus lactis : kinetic properties and factors affecting activation. Journal of Bacteriology 131:82–91
    [Google Scholar]
  6. Dehority B. A. 1971; Carbon dioxide requirement of various species of rumen bacteria. Journal of Bacteriology 105:70–76
    [Google Scholar]
  7. Eisenberg R. J., Elchisak M., Rudd J. 1976; Regulation of lactate dehydrogenase activity in Rothia dentocariosa by fructose 1,6-diphosphate and adenosine 5′-triphosphate. Journal of Bacteriology 126:1344–1346
    [Google Scholar]
  8. Everse J., Kaplan N. O. 1973; Lactate dehydrogenases - structure and function. Advances in Enzymology 37:61–133
    [Google Scholar]
  9. Fell B. F., Kay M, Whitelaw F. G., Boyne R. 1968; Observations on the development of ruminal lesions in calves fed on barley. Research in Veterinary Science 9:458–466
    [Google Scholar]
  10. Gregolin C., Singer T. P. 1963; The lactic dehydrogenase of yeast. III. d(–)-Lactic cytochrome c reductase, a zinc-flavoprotein from aerobic yeast. Biochimica et biophysica acta 67:201–218
    [Google Scholar]
  11. van Gylswyk N. O. 1977; Activation of NAD-dependent lactate dehydrogenase in Butyrivibrio fibrisolvens by fructose 1,6-diphosphate. Journal of General Microbiology 99:441–443
    [Google Scholar]
  12. Hobson P. N. 1965a; Continuous culture of some anaerobic and facultatively anaerobic rumen bacteria. Journal of General Microbiology 38:167–180
    [Google Scholar]
  13. Hobson P. N. 1965b; Continuous culture of rumen bacteria : apparatus. Journal of General Microbiology 38:161–166
    [Google Scholar]
  14. Hobson P. N. 1969; Rumen bacteria. Methods in Microbiology 3B:133–149
    [Google Scholar]
  15. Hobson P. N., Summers R. 1967; The continuous culture of anaerobic bacteria. Journal of General Microbiology 47:53–65
    [Google Scholar]
  16. Hobson P. N., Summers R. 1972; ATP pool and growth yield in Selenomonas ruminantium . Journal of General Microbiology 70:351–360
    [Google Scholar]
  17. Holland R., Pritchard G. G. 1975; Regulation of the l-lactate dehydrogenase from Lactobacillus casei by fructose-1,6-diphosphate and metal ions. Journal of Bacteriology 121:777–784
    [Google Scholar]
  18. Jonas H. A., Anders R. F., Jago G. R. 1972; Factors affecting the activity of the lactate dehydrogenase of Streptococcus cremoris . Journal of Bacteriology 111:397–403
    [Google Scholar]
  19. Kubowitz F., Ott P. 1943; Isolierung und Kristallisation eines Garungsfermentes aus Tumoren. Biochemische Zeitschrift 314:94–117
    [Google Scholar]
  20. Kurihara Y., Eadie J. M., Hobson P. N., Mann S. O. 1968; Relationship between bacteria and ciliate protozoa in the sheep rumen. Journal of General Microbiology 51:267–288
    [Google Scholar]
  21. Latham M. J., Legakis N. J. 1976; Cultural factors influencing the utilization or production of acetate by Butyrivibrio fibrisolvens . Journal of General Microbiology 94:380–388
    [Google Scholar]
  22. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
  23. Morley G., Dawson A., Marks V. 1968; Manual and autoanalyser methods for measuring blood glucose using guaiacum and glucose oxidase. Proceedings of the Association of Clinical Biochemists 5:42–45
    [Google Scholar]
  24. Scheifinger C. C., Latham M. J., Wolin M. J. 1975; Relationship of lactate dehydrogenase specificity and growth rate to lactate metabolism by Selenomonas ruminantium . Applied Microbiology 30:916–921
    [Google Scholar]
  25. Scott H. W., Dehority B. A. 1965; Vitamin requirements of several cellulolytic rumen bacteria. Journal of Bacteriology 89:1169–1175
    [Google Scholar]
  26. Tarmy E. M., Kaplan N. O. 1968; Kinetics of Escherichia coli b d-lactate dehydrogenase and evidence for pyruvate-controlled change in conformation. Journal of Biological Chemistry 243:2587–2596
    [Google Scholar]
  27. de Vries W., Kapteijn W. M. C., van der Beek E. G., Stouthamer A. H. 1970; Molar growth yields and fermentation balances of Lactobacillus casei 13 in batch cultures and in continuous cultures. Journal of General Microbiology 63:333–345
    [Google Scholar]
  28. de Vries W., van Wijck-Kapteyn W. M. C., Oosterhuis S. K. H. 1974; The presence and function of cytochromes in Selenomonas ruminantium, Anaerovibrio lipolytica and Veillonella alcalescens . Journal of General Microbiology 81:69–78
    [Google Scholar]
  29. Wittenberger C. L. 1968; Kinetic studies on the inhibition of a d( – )-specific lactate dehydrogenase by adenosine triphosphate. Journal of Biological Chemistry 243:3067–3075
    [Google Scholar]
  30. Wittenberger C. L., Fulco J. G. 1967; Purification and allosteric properties of a nicotinamide adenine dinucleotide-linked d(–)-specific lactate dehydrogenase from Butyribacterium rettgeri . Journal of Biological Chemistry 242:2917–2924
    [Google Scholar]
  31. Wolin M. J. 1964; Fructose-1,6-diphosphate requirement of streptococcal lactic dehydrogen-ases. Science 146:775–777
    [Google Scholar]
  32. Wolin M. J. 1975; Interactions between the bacterial species of the rumen. Digestion and Metabolism in the RuminantProceedings of the IVth International Symposium on Ruminant Physiology134–148 McDonald I. W., Warner A. C. I., Armidale N.S.W. 2351 Australia: University of New England Publishing Unit;
    [Google Scholar]
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