CHARACTERIZATION OF REDOX PROTEINS FROM EXTREME THERMOPHILIC ARCHAEBACTERIA - STUDIES ON ALCOHOL-DEHYDROGENASE AND THIOREDOXINS

Proteins isolated from extreme thermophilic microorganisms for their g eneral stability to the common protein denaturants (heating, pH, organ ic solvents, urea, SDS, proteases) represent an important development in the potential exploitation of proteins and enzymes for practical pu rposes. Here we report studies on the thermoactivity and thermostabili ty of an alcohol dehydrogenase purified from the extreme thermoacidoph ilic archaebacterium Sulfolobus solfataricus, in the absence and in th e presence of water-miscible organic solvents, as well as studies on e nzyme immobilization and co-enzyme recycling. Three thermostable thior edoxins isolated and purified from Bacillus acidocaldarius, Sulfolobus solfataricus; and Pyrococcus furiosus, have been partially characteri zed.