Thermal properties of enzymes from Bacillus flavothermus, grown between 34 and 70 degrees C.
The activity and stability of several enzymes from the facultative thermophile Bacillus flavothermus, grown within the mesophilic and thermophilic region at 34 degrees C, 43 degrees C, 52 degrees C and 70 degrees 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, glutamate-oxalacetate and glutamate-pyruvate transaminase and myokinase) the intrinsic stability was found to increase to about 55 degrees 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 degrees C and 51 degrees C while the thermal characteristics are not changed below and beyond this crucial region.
D001407:Bacillus / Q000201:enzymology* / Q000254:growth & development; D006358:Hot Temperature; D010088:Oxidoreductases / Q000378:metabolism*; D010770:Phosphotransferases / Q000378:metabolism*; D011489:Protein Denaturation; D000637:Transaminases / Q000378:metabolism*
D010088:Oxidoreductases; D000637:Transaminases; D010770:Phosphotransferases