The influence of-Cu(H2L)Cl] complex on proteolytic activity of T. koningii Oudem. CNMN FD 12 fungal strain was evaluated during the 7-11 days of cultivation. The stimulatory effect of the concentrations of 5-15 mg/L of metal complex on the activity of neutral and acid proteases was observed. The peak of acid and neutral protease activity was determined on the 9th and 10th day of cultivation, similar to the control sample. The most favorable concentration of-Cu(H2L)Cl] was 10 mg/L. Following purification of the proteases by gel filtration resulted in an increase of the specific activity of the control preparation of 1.3-1.7 times for neutral proteases and 1.3-1.8 times for acid proteases. The overall yield, determined for fractions with proteolytic activity, constituted 19% for neutral proteases, and 21% for acid proteases. Purification of the optimized preparation showed an increase in specific activity of the neutral protease of 0.8-1.3 times and of the acid proteases of 1.5-1.7 times. The overall yield was 12.2% for neutral proteases and 18.8% for acid proteases. SDS-PAGE electrophoresis of isolated proteins from the chromatographic fractions showed polypeptide bands only in proteolytic active fractions. Some new polypeptides with apparent molecular mass of 51 and 49 kDa appeared in the polypeptide profile of optimized preparation. The changes were most likely induced by the utilization of [Cu(H2L)Cl] coordination compound in the T. koningii cultivation process.