Abstract
The enzyme alcohol dehydrogenase (ADH) is a dimeric enzyme in which each of its subunits has a Zn2+ metal-containing catalytic domain and a cofactor binding domain. This enzyme converts alcohol into an aldehyde. In this article, the activity of the enzyme was investigated by applying the immobilization process directly to the alcohol dehydrogenase enzyme purified and activated florisil from the chicken liver. For this purpose, homogenization of chicken liver was achieved and its supernatants were separated by applying the ultracentrifugation process to the resulting homogenate. Then, % ammonium precipitation, dialysis, and ion exchange chromatography processes were performed, respectively. As a result of these processes, the hepatic alcohol dehydrogenase was purified 150.3 times compared to the coarse homogenate, and the specific activity of the enzyme was determined to be 0.631 U/mg protein. The activity of the enzyme directly immobilized was found to be 0.034 U/mg protein.
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