ИСТИНА

Formate dehydrogenase (FDH, EC 1.2.1.2.) occurs and plays very important role in different organisms: bacteria, yeasts, fungi and plants. The enzyme is also of high practical interest. It is used for NADH regeneration in processes of fine organic synthesis of chiral compounds with different oxidoreductases. Formate dehydrogenases from different sources are studied in our laboratory and now a new FDH from Staphylococcus aureus (SauFDH) is of our main interest. The gene, encoding SauFDH was successfully cloned. We constructed recombinant E.coli strain and optimized cultivation conditions resulted in the recombinant enzyme yield up to 700 mg per liter. Recombinant SauFDH was purified and characterized. It was found that SauFDH possesses rather high thermal stability, comparable to one for FDH from Pseudomonas sp. 101, which is one of the most stable known FDHs. Although wild type enzyme doesn’t entirely fit practical requirements because of its lower catalytic activity, which can be optimized with protein design.