Characterization of redox proteins from extreme thermophilic archaebacteria: studies on alcohol dehydrogenase and thioredoxins.

Proteins isolated from extreme thermophilic microorganisms for their general stability to the common protein denaturants (heating, pH, organic solvents, urea, SDS, proteases) represent an important development in the potential exploitation of proteins and enzymes for practical purposes. Here we report studies on the thermoactivity and thermostability of an alcohol dehydrogenase purified from the extreme thermoacidophilic archaebacterium Sulfolobus solfataricus, in the absence and in the presence of water-miscible organic solvents, as well as studies on enzyme immobilization and co-enzyme recycling. Three thermostable thioredoxins isolated and purified from Bacillus acidocaldarius, Sulfolobus solfataricus and Pyrococcus furiosus, have been partially characterized.