1887

Abstract

Summary

() ( 418, no. 240) was grown at dilution rates between 0·1 and 1·0 hr in a variety of nutrient-limited chemostats and the activities of dehydrogenases, particularly glucose (R), fructose (R), sucrose (R), maltose (R) and gluconate (R) dehydrogenases, were determined in intact organisms. Their activities varied from system to system, but, with a few exceptions, were largely independent of the dilution rate. R was generally high when sugars provided the carbon for growth but when intermediates of the tricarboxylic acid cycle were used it was often low. R behaved like R but R, R, and R were more variable. In general the activities were higher in C-limitation than in other nutrient-limited conditions.

Specific activities of - and -glucosidase were also determined in some of the systems. Organisms grown in a maltose-limited system had the highest -glucosidase activity but 40% of this level was observed in those from a cellobiose-limited system although cellobiose is a -glucoside. Glucose, fructose, sucrose, lactose or disaccharides containing an 1 → 6 linkage as carbon sources induced little activity. As expected, growth in cellobiose-limited conditions led to high -glucosidase activity but melibiose-grown cells were about 50% as active. Replacing NH , the usual N source in the medium, by NO in a glucose-limited system increased the -glucosidase activity five- to sixfold, while NO led to a tenfold decrease. -Glucosi-dase was less affected.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-57-2-169
1969-08-01
2024-04-26
Loading full text...

Full text loading...

/deliver/fulltext/micro/57/2/mic-57-2-169.html?itemId=/content/journal/micro/10.1099/00221287-57-2-169&mimeType=html&fmt=ahah

References

  1. Birdsell D. C., Cota-Robles E. H. 1967; Production and ultrastructure of lysozyme and ethylenediaminetetracetate-lysozyme spheroplasts of Escherichia coli. J. Bact 93:427
    [Google Scholar]
  2. Clarke P. H., Houldsworth M. A., Lilly M. D. 1968; Catabolite repression and the induction of amidase synthesis by Pseudomonas aeruginosa 8602. J. gen. Microbiol 51:225
    [Google Scholar]
  3. Dalby A., Blackwood A. C. 1955; Oxidation of sugars by an enzyme preparation from Aerobacter aerogenes. Can. J. Microbiol 1:733
    [Google Scholar]
  4. Dean A. C. R., Rogers P. L. 1967; The cell size and macromolecular composition of Aerobacter aerogenes in various systems of continuous culture. Biochim. biophys. Acta 148:267
    [Google Scholar]
  5. Forget P. 1968; Recherches sur le métabolisme du glucose chez les bactéries dénitrificantes. I. Aerobacter aerogenes. Annls Inst. Pasteur, Paris 115:181
    [Google Scholar]
  6. Fox C. F., Wilson G. 1968; The role of a phosphoenolpyruvate-dependent kinase system in β-glucoside catabolism in Escherichia coli. Proc. natn. Acad. SciU.S.A 59988
    [Google Scholar]
  7. Fred R. B., Knight S. G. 1949; The reduction of 2,3,5-triphenyl-tetrazolium chloride by Penicillium chrysogenum. Science, N.Y 109:169
    [Google Scholar]
  8. Grant D. J. W., Hinshelwood C. 1964; Studies of the enzyme activity of Bact. lactis aerogenes Aerobacter aerogenes). I. The effects of cellular disruption on the activities of some typical enzymes. Proc. R. Soc. B 16025
    [Google Scholar]
  9. Gunsalus I. C., Horecker B. L., Wood W. A. 1955; Pathways of carbohydrate metabolism in micro-organisms. Bact. Rev 19:79
    [Google Scholar]
  10. Hamlin B. T., Ng F. M.-W., Dawes E. A. 1967; Regulation of enzymes of glucose metabolism in Pseudomonas aeruginosa by citrate. In Microbial Physiology and Continuous Culture Powell E. O., Evans C. G. T., Strange R. E., Tempest D. W. 211 London: H.M.S.O;
    [Google Scholar]
  11. Hayashi M., Hayashi M., Unemoto T. 1966; The presence of d-malate dehydrogenase (d-malate: NAD oxidoreductase) in Serratia marcescens. Biochim. biophys. Acta 122:374
    [Google Scholar]
  12. Henning U., Dietrich J., Deppe G. 1968; Regulation of the synthesis of Escherichia coli pyruvate dehydrogenase. Biochem. J 106:25
    [Google Scholar]
  13. Lin E. C. C. 1961; An inducible d-arabitol dehydrogenase from Aerobacter aerogenes. J. biol. Chem 236:31
    [Google Scholar]
  14. Liss M., Horwits S. B., Kaplan N. O. 1962; d-mannitol-1-phosphate dehydrogenase and d-sorbitol-1-phosphate dehydrogenase in Aeorbacter aerogenes. J. biol. Chem 237:1342
    [Google Scholar]
  15. Málek I. 1969Proceedings 4th International Symposium on continuous culture of micro-organisms Prague, 1968 Folio microbiol., Praha (in the Press)
    [Google Scholar]
  16. Monod J., Cohen-Bazire G., Cohn M. 1951; Sur la biosynthese de la β-galactosidase (lactase) chez Escherichia coli. La specificity de l’induction. Biochitn. biophys. Acta 7:585
    [Google Scholar]
  17. Moses V., Sharp P. B. 1968; Studies on the regulation of glucose-metabolizing enzymes in Bacillus subtilis. J. gen. Microbiol 52:391
    [Google Scholar]
  18. Pirt S. J. 1967; Steady state conditions for synthesis of exocellular products. In Microbial Physiology and Continuous Culture Powell E. O., Evans C. G. T., Strange R. E., Tempest D. W. 162 London: H.M.S.O;
    [Google Scholar]
  19. Schaefler S., Schenkein I. 1968; β-glucoside permeases and phospho-β-glucosidases in Aerobacter aerogenes. Relationship with cryptic phospho-β-glucosidases in Enterobacteriaceae. Proc. natn. Acad. SciU.S.A 59285
    [Google Scholar]
  20. Tanaka S., Lerner S. A., Lin E. C. C. 1967; Replacement of a phosphoenolpyruvate-dependent phosphotransferase by a nicotinamide adenine dinucleotide-linked dehydrogenase for the utilization of mannitol. J. Bact 93:642
    [Google Scholar]
  21. Tempest D. W., Herbert D. 1965; Effect of dilution rate and growth-limiting substrate on the metabolic activity of Torula utilis. J. gen. Microbiol 41:143
    [Google Scholar]
  22. Wright D. N., Lockhart W. R. 1965; Effects of growth rate and limiting substrate on glucose metabolism in Escherichia coli. J. Bact 89:1082
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-57-2-169
Loading
/content/journal/micro/10.1099/00221287-57-2-169
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