Catalase belongs to the class of oxidoreductases; it catalyzes the decomposition of hydrogen peroxide formed during biological oxidation, and also oxidizes low molecular weight alcohols and nitrites in the presence of hydrogen peroxide. This high molecular weight chromoprotein (Mw 250, pI 5.4) consists of four identical subunits that do not have catalytic activity and has oxidized heme as a prosthetic group. The optimum catalytic activity of the catalase occurs at pH 6.8-7.0. The enzyme is used in the textile and food industries, [1] in wastewater treatment, [2] in cosmetics and pharmaceuticals, [3] as well as in analytical biotechnology to determine the amount of hydrogen peroxide. [3b] Determination of the enzyme activity in human erythrocytes is used in medicine for the diagnostics of blood diseases.The industrial application of the catalase is significantly hampered by a lack of longterm operational stability and technical difficulties with the reuse of the enzyme. [3b] In this respect, the immobilization of the catalase on insoluble carriers represents an important practical task, since it allows overcoming the drawbacks of low enzymatic stability under unfavorable environmental conditions, during storage and upon repeated use. [3b] Nevertheless, it is important to recognize the limitations of immobilized enzymes, such as typically lower enzyme activity and reaction rates compared to the native enzyme and additional