Investigation of catalase activities from Anoxybacillus gonensis Z4 strain and whole cell immobilization

In this study, the capacity of Anoxybacillus gonensis Z4 strain that were isolated by a research group in the Department of Molecular Biology and Genetics of Faculty of Science of Atatürk University to produce catalase, an industrial enzyme, was investigated, and some kinetic parameters and spectroscopic properties of this catalase enzyme were determined. In addition, Anoxybacillus gonensis Z4 strain was performed immobilization of its whole cell in agar and agarose environments, and their catalase activities were characterized.The catalase-producing ability of this thermophilic species was explored by petri test and native electrophoresis. The catalase from Anoxybacillus gonensis Z4 strain exhibited the highest activity at pH 7.0 and 50 oC. Catalase from the Z4 thermophilic strain in the presence H2O2 substrate was determined Vmax value as 250,000±980 U / mg protein and the Km value as 17.5±2.2 mM as a result of the kinetic study. In addition, catalase from thermophilic Z4 strain, using in this study, was inhibited by NaN3, KCN, HgCl2, and 3-amino-1,2,4-triazole known catalase inhibitors.The catalase obtained from Anoxybacillus gonensis Z4 strain was observed to give Soret peak showing the heme group only 410 nm in natural state, and to give Soret peak 415 nm, ?-band and ß-band peaks around 520-550 nm with KCN.Agar and agarose were used for whole cell immobilization of the study. Immobilized cells showed the activity of catalase and it has 50000±413 U / g gel as Vmax value and 200±28 mM as Km value. It was observed that catalase activity was maintained 80% by cells immobilized in agarose media and 53% by cells immobilized in agar media in the use of the second.In conclusion, Anoxybacillus gonensis Z4 strain tested in this study was found, because of its high catalase activity, to be a potential source of catalase for the industries utilizing hydrogen peroxide.