Adiyaman city, which is located in the north of the Ataturk Dam Lake, has no wastewater purification facilities which results in municipal, agricultural, and industrial wastewater discharges directly entering the reservoir. To assess the pollution in the dam lake, we used several oxidative stress biomarkers in blood tissue of Cyprinus carpio. Fish samples were taken from Sitilce, polluted area by untreated wastewaters, and Samsat, relatively clean area, in the reservoir in August 2012. The activity of catalase and level of malondialdehyde increased while activity of superoxide dismutase and glutathione level decreased in fish from Sitilce site when compared to Samsat site. The findings of the present investigation suggest that the presence of certain prooxidative compounds that can lead to oxidative stress in the fish at the Sitilce site and oxidative stress biomarkers may be important in order to evaluate the effects of untreated wastewaters on living organisms in the dam lake.

This study investigated if the use of the pesticides cyprodinil and fludioxonil produced an inhibitory effect on the bovine liver catalase (CAT) activity. It was documented that the activity of the enzyme decreased with increasing concentrations of cyprodinil and fludioxonil from 0 to 500 ppm. At pesticide concentrations of 250 and 500 ppm, the activity of CAT remained unchanged and passed to a steady state. The exposure to cyprodinil in concentrations of 10, 50, 100, 250 and 500 ppm, led to a decrease in the per cent of the CAT enzyme activity calculated as 45.4, 68.0, 73.0, 77.8 and 77.4, respectively. Similarly, the exposure to fludioxonil in concentrations of 10, 50, 100, 250 and 500 ppm, produced the following percentage decrease in the CAT enzyme activity: 20.0, 30.8, 42.8, 46.3 and 45.9, respectively. Cyprodinil inhibited CAT competitively, whereas the mechanism of fludioxonil inhibition over the enzyme was non-competitive.

Soybean lipoxygenase (Lox) was covalently immobilized onto polyacrylamide gel which activated with glutaraldehyde. Optimal temperature for free enzyme was 30 °C whereas for the immobilized lipoxygenase (Imm-Lox) optimal temperature increased to 35 °C. The optimal pH for free enzyme and immobilized enzyme was 10.5 and 8.5, respectively. The maximum activity of Imm-Lox was low as compared with that of free soybean lipoxygenase. The reusability of Imm-Lox was investigated after 7 uses; enzyme retained 85 % of its original activity. Storage stability of Imm-Lox was tested at different conditions.

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