General stability of thermophilic enzymes: studies on 6-phosphogluconate dehydrogenase from Bacillus stearothermophilus and yeast.
The thermophilic enzyme 6-phosphogluconate dehydrogenase (6-phospho-D-gluconate:NADP oxidoreductase, decarboxylating, EC 1.1.1.44) from Bacillus stearothermophilus was much more resistant to inactivation under different conditions of temperature, pH, guanidine-hydrochloride, and organic solvents (dioxane, dimethylformamide, acetone) than its mesophilic counterpart from yeast. In addition, the thermophilic enzyme largely withstands proteolysis with trypsin, chymotrypsin, and elastase when compared with the yeast enzyme. It is proposed that thermophilic enzymes are not only thermostable, but also generally more stable to most common protein denaturants than their mesophilic counterparts. Because of their remarkable stability, enzymes isolated from thermophilic microorganisms may be ideally suited for technological applications.
D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D010447:Peptide Hydrolases / Q000494:pharmacology; D010734:Phosphogluconate Dehydrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011489:Protein Denaturation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D010734:Phosphogluconate Dehydrogenase; D010447:Peptide Hydrolases