Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Thermal properties of enzymes from Bacillus flavothermus, grown between 34 and 70°C

  • 57 Accesses

  • 12 Citations


The activity and stability of several enzymes from the facultative thermophile Bacillus flavothermus, grown within the mesophilic and thermophilic region at 34°C, 43°C, 52°C and 70°C, have been examined. While the temperature optima and maxima of all enzymes tested were found to remain unchanged at all growth temperatures, it was demonstrated that the heat stability of the proteins increased with ten perature, however, not uniformly for all enzymes. One exception was acetate kinase and the intrinsic stability of pyruvate kinase was found to increase only slightly. With all other proteins tested (alanine dehydrogenase, isocitric dehydrogenase and glucose-6-phosphate dehydrogenase, glutamateoxalacetate and glutamate-pyruvate transaminase and myokinase) the intrinsic stability was found to increase to about 55°C, but stayed unaltered at higher growth temperatures. Except for acetate kinase and myokinase, the enzymes could be stabilized by their respective substrates and the heat stability of the ES-complexes was found also to depend on the growth temperature of the cells. These data lead to the conclusion that the enzymes undergo a transition from heat-labile to thermostable within the growth temperature range between 44°C and 51°C while the thermal characteristics are not changed below and beyond this crucial region.

This is a preview of subscription content, log in to check access.


  1. Amelunxen, R. and Lins, M. 1968. Comparative thermostability of enzymes from Bacillus stearothermophilus and Bacillus cereus.—Arch. Biochem. Biophys. 125: 765–769.

  2. Barnes, E. M., Akagi, J. M. and Himes, R. H. 1971. Properties of fructose-1,6-diphosphate aldolase from two thermophilic and mesophilic Clostridia.—Biochim. Biophys. Acta 227: 199–203.

  3. Brown, D. K., Militzer, W. and Georgi, C. E. 1957. The effect of growth temperature on the heat stability of a bacterial pyrophosphatase.—Arch. Biochem. Biophys. 70: 248–256.

  4. Fernald, N. and Ramaley, R. 1972. Purification and properties of succinyl-CoA-synthetase isolated from Bacillus subtilis 168, Bacillus stearothermophilus and Thermus aquaticus.—Arch. Biochem. Biophys. 153: 95–102.

  5. Frank, G., Haberstich, H. U., Schaer, H. P., Tratschin, J. D. and Zuber, H. 1976. Thermophilic and mesophilic enzymes from B. caldotenax and B. stearothermophilus: Properties, relationships and formation. p. 375–389. In H. Zuber (ed.), Enzymes and proteins from thermophilic microorganisms—Birkhäuser Verlag, Basel, Stuttgart.

  6. Haberstich, H. U. and Zuber, H. 1974. Thermoadaptation of enzymes in thermophilic and mesophilic cultures of Bacillus stearothermophilus and Bacillus caldotenax.—Arch. Microbiol. 98: 275–287.

  7. Heinen, W., Lauwers, A. M. and Mulders, J. W. M. 1982. Bacillus flavothermus, a newly isolated facultative thermophile.—Antonie van Leeuwenhoek 48: 265–272.

  8. Jung, L., Jost, R., Stoll, E. and Zuber, H. 1974. Metabolic differences in Bacillus stearothermophilus grown at 55° C and 37° C.—Arch. Microbiol. 95: 125–138.

  9. Lauwers, A. M., Heinen, W. and Mulders, J. W. M. 1981. Properties of enzymes from bacteria grown in the 70–100° C range.—Arch. Microbiol. 130: 159–164.

  10. Middaugh, C. R. and Mac Elroy, R. D. 1976. The effect of temperature on ribose-5-phosphate isomerase from a mesophile, Thiobacillus thioparus, and a thermophile, Bacillus caldolyticus.—J. Biochem. 79: 1331–1344.

  11. O'Brien, W. E., Brewer, J. M. and Ljungdahl, L. G. 1976. Chemical, physical and enzymatic comparisons of formyltetrahydrofolate synthetases from thermo- and mesophilic Clostridia. p. 249–262. In H. Zuber (ed.), Enzymes and proteins from thermophilic microorganisms.—Birkhäuser Verlag, Basel, Stuttgart.

  12. Perutz, M. F. 1978. Electrostatic effects in proteins.—Science 201: 1187–1191.

  13. Shing, Y. W., Akagi, J. M. and Himes, R. H. 1975. Psychrophilic, mesophilic and thermophilic triosephosphate isomerases from three clostridial species.—J. Bacteriol. 122: 177–184.

  14. Wedler, F. C., Hoffmann, F. M., Kenny, R. and Carfi, J. 1976. Maintenance of specificity, information, and thermostability in thermophilic Bacillus sp. glutamine synthetase. p. 187–197. In H. Zuber (ed.), Enzymes and proteins from thermophilic microorganisms.—Birkhäuser Verlag, Basel, Stuttgart.

Download references

Author information

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Lauwers, A.M., Heinen, W. Thermal properties of enzymes from Bacillus flavothermus, grown between 34 and 70°C. Antonie van Leeuwenhoek 49, 191–201 (1983). https://doi.org/10.1007/BF00393678

Download citation


  • Pyruvate
  • Alanine
  • Growth Temperature
  • Pyruvate Kinase
  • Thermal Characteristic