1887

Abstract

SUMMARY

Three psychrophilic micro-organisms (strains of Arthrobacter, Candida and ) were capable of growth for a period when exponential-phase cultures in chemically defined media were transferred from temperatures at or near the optima for growth (20, 10 and 15°, respectively), to 37,25 and 30°, respectively. The latter temperatures were 3–5° above the maxima for the growth of the organisms in freshly inoculated cultures. Growth at the higher temperatures was greatest with the Candida and least with the Arthrobacter. Cultures of the Arthrobacter and Candida grew when transferred back to the optimum temperatures for growth, after a lag which increased with the length of time that the cultures had spent at the higher temperatures. cultures grew almost immediately after they were transferred back to the optimum growth temperature. Growth of the organisms at the higher temperatures was not affected by supplementing cultures with bacteriological peptone and/or yeast extract. There was a rapid decline in the viability and in the rates of respiration of endogenous reserves and of exogenous glucose and pyruvate when Arthrobacter and Candida cultures were transferred to the higher temperatures. But with the respiratory activities were not so markedly affected by the change in incubation temperature, while the viability of this bacterium increased slightly after the transfer of cultures to the higher temperature. The activities of many of the tricarboxylic acid cycle enzymes in Arthrobacter and Candida were diminished after the transfer of organisms from the optimum temperature to one above the maximum for growth; but the activities of these enzymes in were less affected by the change in incubation temperature. There was no marked intracellular accumulation or excretion of ultraviolet-absorbing compounds by the organisms after the transfer of cultures to the higher temperatures. The results are discussed in relation to the biochemical factors which may determine the maximum temperatures for growth of these organisms.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-40-3-349
1965-09-01
2024-04-25
Loading full text...

Full text loading...

/deliver/fulltext/micro/40/3/mic-40-3-349.html?itemId=/content/journal/micro/10.1099/00221287-40-3-349&mimeType=html&fmt=ahah

References

  1. Ahmad F., Rose A. H. 1962; The role of biotin in the regulation of enzyme synthesis in yeast. Arch. Biochem. Biophys 28:147
    [Google Scholar]
  2. Ahmad F., Rose A. H., Garg N. K. 1961; Effect of biotin deficiency on the synthesis of nucleic acids and protein by Saccharomyces cerevisiae . J. gen. Microbiol 24:69
    [Google Scholar]
  3. Beaufay H., Bendall D. S., Baudhuin P., De Duve C. 1959; Tissue fractionation studies. 12. Intracellular distribution of some dehydrogenases, alkaline deoxyribo- nuclease and iron in rat-liver tissue. Biochem. J 73:624
    [Google Scholar]
  4. Bernath P., Singer T. 1962; Succinic dehydrogenase. In Methods in Enzymology 5597 Colowick S. P., and Kaplan N. O. New York: Academic Press;
    [Google Scholar]
  5. Brown A. D. 1957; Some general properties of a psychrophilic pseudomonad: the effects of temperature on some of these properties and the utilization of glucose by this organism and Pseudomonas aeruginosa . J. gen. Microbiol 17:640
    [Google Scholar]
  6. Burton S. D., Morita R. Y. 1963; Denaturation and renaturation of malic dehydrogenase in a cell-free extract from a marine psychrophile. J. Bact 86:1019
    [Google Scholar]
  7. Byrne P., Chapman D. 1964; Liquid crystalline nature of phospholipids. Nature, Lond 202:987
    [Google Scholar]
  8. Califano L. 1952; Libération d’acide nucléique par les cellules bactériennes sous l’action de la chaleur. Bull. Wld Hlth Org 6:19
    [Google Scholar]
  9. Chick H. 1910; The process of disinfection by chemical agencies and hot water. J. Hyg., Camb 10:237
    [Google Scholar]
  10. Edwards O. F., Rettger L. F. 1937; The relation of certain respiratory enzymes to the maximum growth temperatures of bacteria. J. Bact 34:489
    [Google Scholar]
  11. Gomori G. 1955; Preparation of buffers for use in enzyme studies. Meth. Enzymol 1:138
    [Google Scholar]
  12. Hagen P-O., Rose A. H. 1961; A psychrophilic cryptococcus. Canad. J. Microbiol 7:287
    [Google Scholar]
  13. Hagen P-O., Kushner D. J., Gibbons N. E. 1964; Temperature-induced death and lysis in a psychrophilic bacterium. Canad. J. Microbiol 10:813
    [Google Scholar]
  14. Hagen P-O., Rose A. H. 1962; Studies on the biochemical basis of the low maximum temperature in a psychrophilic eryptococcus. J. gen Microbiol 27:89
    [Google Scholar]
  15. Horecker B. L., Kornberg A. 1948; The extinction coefficients of the reduced band of pyridine nucleotides. J. biol. Chem 175:385
    [Google Scholar]
  16. Jaganathan V., Schweet R. S. 1952; Pyruvic oxidase of pigeon breast muscle. I. Purification and properties of the enzyme. J. biol. Chem 196:551
    [Google Scholar]
  17. Kates M., Hagen P-O. 1964; Influence of temperature on fatty acid composition of psychrophilic and mesophilic Serratia species. Canad. J. Biochem. Physiol 42:481
    [Google Scholar]
  18. Kornberg G. A., Pricer W. E. 1951; Di- and triphospho-pyridine nucleotide isocitric dehydrogenases in yeast. J. biol. Chem 189:123
    [Google Scholar]
  19. Langridge J. 1963; Biochemical aspects of temperature response. Annu. Rev. plant Physiol 14:441
    [Google Scholar]
  20. Lipmann F., Tuttle L. C. 1945; A specific micromethod for the determination of acyl phosphates. J. biol. Chem 159:21
    [Google Scholar]
  21. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin reagent. J. biol. Chem 193:265
    [Google Scholar]
  22. Luzzati V., Husson F. 1962; The structure of the liquid crystalline phases of lipid water systems. J. Cell Biol 12:207
    [Google Scholar]
  23. Marmur J., Doty P. 1959; Heterogeneity in deoxyribonucleic acids. I. Dependence on composition of the configurational stability of deoxyribonucleic acids. Nature, Lond 183:1427
    [Google Scholar]
  24. Mickle H. 1948; Tissue disintegrator. J.R. micr. Soc 68: Series III 10
    [Google Scholar]
  25. Militzer W., Burns L. 1954; Thermal enzymes. VI. Heat stability of pyruvic oxidase. Arch. Biochem. Biophys 52:66
    [Google Scholar]
  26. Morita R. Y., Burton S. D. 1963; Influence of moderate temperature on growth and malic dehydrogenase activity of a marine psychrophile. J. Bact 86:1025
    [Google Scholar]
  27. Northam B. E., Norris F. W. 1951; Growth requirements of Schizosaccharomyces octosporus, a yeast exacting towards adenine. J. gen. Microbiol 5:502
    [Google Scholar]
  28. Ochoa S. 1948; Biosynthesis of tricarboxylic acids by carbon dioxide fixation. III. Enzymatic mechanisms. J. Hoi. Chem 174:133
    [Google Scholar]
  29. Ochoa S. 1955a; Malic dehydrogenase from pig heart. Meth. Enzymol 1:735
    [Google Scholar]
  30. Ochoa S. 1955b; Crystalline condensing enzyme from pig heart. Meth. Enzymol 1:685
    [Google Scholar]
  31. Racker E. 1950; Spectrophotometric measurements of the enzymatic formation of fumaric and cis-aconitic acids. Biochim. biophys. Acta 4:221
    [Google Scholar]
  32. Ramakrishnan C. V., Martin S. M. 1954; The enzymatic synthesis of citric acid by cell-free extracts of Aspergillus niger. Canad . J. Biochem. Physiol 32:434
    [Google Scholar]
  33. Rose A. H., Evison L. M. 1965; Studies on the biochemical bases of the minimum temperatures for growth of certain psychrophilic and mesophilic micro-organisms. J. gen. Microbiol 38:131
    [Google Scholar]
  34. Rose A. H., Nickerson W. J. 1956; Secretion of nicotinic acid by biotin-dependent yeasts. J. Bact 72:324
    [Google Scholar]
  35. Sanadi D. R., Littlefield J. W., Bock R. M. 1952; Studies on a-ketoglutaric oxidase. II. Purification and properties. J. biol. Chem 197:851
    [Google Scholar]
  36. Strange R. E., Shon M. 1964; Effect of thermal stress on the viability and ribo- nucleic acid of Aerobader aerogenes in aqueous suspension. J. gen. Microbiol 34:99
    [Google Scholar]
  37. Tucker R. G. 1960; The oxidation of tricarboxylic acid cycle intermediates by a strain of Corynebaderium erythrogenes . J. gen. Microbiol 23:267
    [Google Scholar]
  38. Umbreit W. W., Burris R. H., Stauffer J. F. 1964 Manometric Techniques, 4. Minneapolis: Burgess Publishing Company;
    [Google Scholar]
  39. Upadhyay J., Stokes J. L. 1963; Temperature-sensitive formic hydrogenlyase in a psychrophilic bacterium. J. Bact 85:177
    [Google Scholar]
  40. Williams P. J. le B., Rainbow C. 1964; Enzymes of the tricarboxylic acid cycle in acetic acid bacteria. J. gen. Microbiol 35:237
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-40-3-349
Loading
/content/journal/micro/10.1099/00221287-40-3-349
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