Purification and biochemical characterization of the glutathione reductase enzyme from worm compost

Glutathione is a very important metabolite that takes part in intracellular metabolic processes. The enzyme glutathione reductase makes an important contribution to the maintenance of its intracellular level. In this study, it was aimed to purify and biochemically characterize glutathione reductase enzyme from the earthworm species Eisenia fetida and to investigate the effect of some soil polluting metals on enzyme activity. At the end of the thesis study, the enzyme was purified 397 times. The optimum pH of the enzyme was found to be 8.5 and the optimum ionic Tris buffer was 75 mM. While the temperature at which the enzyme shows optimum activity was determined as 40 0C, it was determined that the enzyme kept its activity at the same temperature. Km and Vmax values of the enzyme against substrate and coenzyme were determined. The inhibition effect of Pb+2, Cu+2, Fe+3 and Zn+2 ions on enzyme activity was observed.