مریم مهاجرانی

The presence of asparaginase as an enzyme that hydrolyzes asparagine to aspartic acid has been reported in various organisms including animals, plants and microorganisms other than humans. This enzyme plays an important role in cellular metabolism in the metabolism of most organisms. On the other hand, its use in food industry reduces acrylamide in food products related to it. In addition, the enzyme L-asparaginase plays an important role in the treatment of acute lymphoblastic leukemia. According to the reported sensitivities of L-asparaginase enzyme extracted from microbial sources in different individuals, the aim of this study was to extract and evaluate of the properties of L-asparaginase enzyme from animal sources such as Muscovy duck liver. For this purpose, duck liver's asparaginase enzyme was partially isolated using homogenization, centrifugation, ammonium sulfate precipitation and dialysis at 4 °C and then the enzyme activity was estimated according to the general generation method with generator reagent. Finally, the function of the enzyme at different temperatures and pH as well as the presence of ions and some effective plant compounds were evaluated. Based on the obtained results, the specific activity of asparaginase enzyme isolated from duck liver was determined to be 2.97 U/mg. The optimal pH of enzyme activity was 7.5 and its optimal temperature was estimated to be 37 °C. The effect of ions and different plant compounds also showed a decreasing effect on enzyme function in all cases, which among ions, calcium and among plant compounds, caffeine, the most reduction was 68.3 and 77.7%, respectively. Dihydroxyflavone and quercetin had the least effect on asparaginase activity and zinc ion maintained enzyme activity. Because access to this enzyme from microbial sources has been reported to limit patients, including the onset of allergy symptoms, extraction of the enzyme from animal sources such as duck liver is not only an affordable and inexpensive s