Archives of Microbiology

, Volume 98, Issue 1, pp 275–287 | Cite as

Thermoadaptation of enzymes in thermophilic and mesophilic cultures of Bacillus stearothermophilus and Bacillus caldotenax

  • H. -U. Haberstich
  • H. Zuber


  1. 1.

    Bacillus stearothermophilus was adapted to 37° C (mesophilic culture) and to 55° C (thermophilic culture) by cultivation via an intermediate temperature of 46° C. In the crude extract of the thermophilic bacterial cells the glucokinase, glucose-6-phosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase and isocitrate dehydrogenase are more thermostable than the corresponding enzymes in the crude extract of mesophilic cells. At the intermediate temperature of 46° C both types are probably formed.

  2. 2.

    37° C-precultures of Bacillus caldotenax were further cultivated (in different samples) at 5° C intervals between 30° C and 70° C. It was shown that in 70° C-cells of the above mentioned enzymes more thermostable forms and in 37° C-cells more thermolabile forms are present.

    Furthermore, as demonstrated in the case of glucose-6-phosphate isomerase and isocitrate dehydrogenase, cells cultured in the temperature range between 30–50° C produced thermolabile enzyme variants (M-type), while cultures between 60–70° C produced thermostable variants (Th-type). At cultivation temperatures above 50° C a pronounced lag-period expressing the metabolic changes was found. In the lag-period, mesophilic enzymes are no longer present as early as 20 min after increasing the temperature (70° C), and synthesis of thermostable enzymes starts about 1 h before the beginning of growth.

  3. 3.

    Similar results were obtained with Bacillus caldotenax precultivated at 70° C and cultivated between 30° C and 70° C.


Key words

Thermophilic bacteria B. stearothermophilus B. caldotenax Thermophilic (Thermostable) Enzymes Adaptation Thermoadaptation of Enzymes Thermoadaptation of Bacteria 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Bausum, H. T., Matney, Th. S.: Boundary between bacterial mesophilism and thermophilism. J. Bact. 90, 50–53 (1965)Google Scholar
  2. Campbell, L. L.: The growth of an “obligate” thermophilic bacterium at 36° C. J. Bact. 68, 505–507 (1954)Google Scholar
  3. Campbell, L. L.: Purification and properties of an α-amylase from facultative thermophilic bacteria. Arch. Biochem. Biophys. 54, 154–161 (1955)Google Scholar
  4. Campbell, L. L., Pace, B.: Physiology of growth at high temperatures. J. appl. Bact. 31, 24–35 (1968)Google Scholar
  5. Dowben, R. M., Weidenmüller, R.: Adaptation of mesophilic bacteria to growth at elevated temperatures. Biochim. biophys. Acta (Amst.) 158, 255–261 (1968)Google Scholar
  6. Gornall, A. G., Baradwill, C. J., David, M. M.: Determination of serum proteins by means of the Biuret reaction. J. biol. Chem. 177, 751–774 (1949)Google Scholar
  7. Heinen, W.: Growth conditions and temperature-dependent substrate specificity of two extremely thermophilic bacteria. Arch. Mikrobiol. 76, 2–17 (1971)Google Scholar
  8. Heinen, V. J., Heinen, W.: Characteristics and properties of a caldo-active bacterium producing extracellular enzymes and two related strains. Arch. Mikrobiol. 82, 1–23 (1972)Google Scholar
  9. Hengartner, H., Zuber, H.: Isolation and characterization of a thermophilic glucokinase from Bacillus stearothermophilus. FEBS Letters 37, 212–216 (1973)Google Scholar
  10. Jung, L., Jost, R., Stoll, E., Zuber, H.: Metabolic differences in Bacillus stearothermophilus grown at 55° C and 37° C. Arch. Microbiol. 95, 125–138 (1974)Google Scholar
  11. Long, S. K., Williams, O. B.: Growth of obligate thermophiles at 37° C as a function of the cultural conditions employed. J. Bact. 77, 545–547 (1959)Google Scholar
  12. Muramatsu, N., Yoshiaki, N.: Purification and characterization of glucose-6-phosphate isomerase from Bacillus stearothermophilus. Arch. Biochem. Biophys. 144, 245–252 (1971)Google Scholar
  13. Ochoa, S.: Biosynthesis of tricarboxylic acids by carbon dioxide fixation. J. biol. Chem. 174, 133–157 (1948)Google Scholar
  14. Roe, J. H.: A calorimetric method for the determination of fructose in blood and urine. J. biol. Chem. 107, 15–22 (1934)Google Scholar
  15. Sidler, W., Zuber, H.: Neutral proteases with different thermostabilities from a facultative strain of Bacillus stearothermophilus grown at 40° C and 50° C. FEBS Letters 25, 292–294 (1972)Google Scholar
  16. Slein, M. W., Cori, G. T., Cori, C. F.: A comparative study of Hexokinase from yeast and animal tissues. J. biol. Chem. 186, 763–780 (1950)Google Scholar
  17. Stoll, E., Hermodson, M. A., Ericsson, L. H., Zuber, H.: Subunit structure of the thermophilic aminopeptidase I from Bacillus stearothermophilus. Biochemistry 11, 4731–4735 (1972)Google Scholar
  18. Warburg, O., Christian, W.: Isolierung und Kristallisation des Proteins des oxydierenden Gärungsferments. Biochem. Z. 303, 40–68 (1939)Google Scholar
  19. Zuber, H., Stoll, E., Balerna, M., Jung, L., Sidler, W.: Thermophilic and mesophilic enzymes from B. stearothermophilus. Abstracts 9th Intern. Congress Biochem., Stockholm 1973Google Scholar

Copyright information

© Springer-Verlag 1974

Authors and Affiliations

  • H. -U. Haberstich
    • 1
  • H. Zuber
    • 1
  1. 1.Institut für Molekularbiologie und Biophysik der Eidgenössischen Technischen HochschuleZürich

Personalised recommendations