Purification of Alcohol Dehydrogenase Enzyme from Chicken Liver and Immobilization Onto Florisil

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