Some of the enzymes of the wild type Micrococcus sp. strain Gl were detected & it was found that strain Gl was positive for catalase <§c nitratase, then depending on a comparison of intracellular activities for each of catalase & protease enzyme in different NaCl concentrations (2, 10 & 20 %), catalase was choosed for the present study according to its importance & its highest production in all NaCl concentrations. However maximal function of catalase obtained from cells grown in 10 % NaCl as compared with catalase produced from 2 % & 20% NaCl grown cells. The enzyme was yielded maximal activity of 89 U/ml when extracted using lysozyme treatment compared with low or no activity resulted from sonication, freezing &thawing of the cells. In addition to studying the effect of extraction methods on catalase activity. The effects of different extraction conditions such as lysozyme, EDTA concentrations & time of incubation on enzyme activity were determined & it seems that 1 mg/ml lysozyme, 1 mM EDTA for 30 min. incubation represents the optimal conditions for complete cell wall lysis. Optimum conditions for the production using YMC medium were investigated & it was found that, an initial medium pH of 7-7.5 using cells grown to mid log phase (O.D600= 0.6), incubation at 40°C with 12 g/1 yeast extract & 4 g/I casein hydrolysate as carbon & nitrogen source in the production medium were the best conditions. The sensitivity Micrococcus sp. strain Gl to hydrogen peroxide –(H2O2) was tested when cultures of strain, Gl pretreated with sublethal doses c: H2O2 exhibited higher levels of catalase activity of bout 195 U/mg rrotein in 10 mM HzOz treated cells. The enzyme purification was carried out through two purification steps including concentration by sucrose & gel filtration on Sepharose 4B column. The overall purification fold was 5.2 with 50.4 % yield. The purity of the enzyme was confirmed by SDS-polyacrylamide gel electrophoresis under denaturing conditions & we have obtained one band of protein. The characterization of the purified enzyme showed that the. optimal pH for activity was 7-7.5 & the enzyme was stable at pH values ranging from (6-7.5). The purified enzyme retained its i activity at (30-45°C) after 15 min. incubation, while all of the activity was lost after 15 min. incubation at 60°C. The enzyme also retained its original activity for up to 50 min. when incubated at 40°C. The effects of some salts such as NaCl, KC1, NH4C1, CaCh & MgCk on enzyme activity were examined & the result showed that the purified enzyme was activated by such environmental stresses such as NaCl, KC1, CaCh & NH4C1 in different manner. The catalytic activity of the purified catalase was found to be inhibited by 70, 74 & 79 % after incubation for 15 min. with 0.05, 0.1 & 0.2 mM sodium azide respectively while treatment with 1,3 & 5 mM EDTA for 15 min. showed 10.4, 20 & 20 % lose of activity indicating that this enzyme was a metallo-enzyme.