A comparative study on the heat stability of triosephosphate isomerase in psychrophilic, psychrotrophic, and mesophilic clostridia.
The temperature stability of triosephosphate isomerase (EC 5.3.1.1) in the cell-free extracts of psychrophilic, psychrotrophic, and mesophilic Clostridium species has been investigated. Even though this enzyme was found to be heat labile in the psychrophilic isolates, no detectable loss in activity was evident when cell-free extracts were heated for 1/2 h at the maximum temperature of growth for the organisms. Two organisms, each with a maximum growth temperature of 23 degrees C, showed different heat stability of triosephosphate isomerase. However, a trend is evident that as the maximum growth temperature increases, the thermostability also increases. It is suggested that the heat liability of this enzyme is not a controlling factor in psychrophilism, but rather an adaptation to the cold habitat of these organisms.
D000222:Adaptation, Physiological; D002238:Carbohydrate Epimerases / Q000378:metabolism*; D002474:Cell-Free System; D003013:Clostridium / Q000201:enzymology* / Q000254:growth & development; D003016:Clostridium perfringens / Q000201:enzymology / Q000254:growth & development; D004355:Drug Stability; D006358:Hot Temperature; D013045:Species Specificity; D013696:Temperature; D014305:Triose-Phosphate Isomerase / Q000378:metabolism*
D002238:Carbohydrate Epimerases; D014305:Triose-Phosphate Isomerase