The results of studies on producing the biocatalyst based on catalase immobilized in the fibers from triacetate are presented. The catalase producer is Penicillium fungus. Catalase was produced by precipitation with the use of ethyl alcohol from the cultural fluid with separate and unseparate mycelium. The highest activity of catalase in the cultural fluid is seen on the nutrient medium containing 4% of carbon source. For immobilization the water solution of enzyme was concentrated in the vacuum-rotor evaporator at temperature of 25 degrees C. The enzyme was included in the structure of fibers during the process of their formation. Of the fiber-producing polymers (cellulose triacetate, chlorine, polysulphone) the most enzymatic activity has the catalase-containing fibers derived from the cellulose triacetate, in this case, the fine fibers of biocatalyst have the higher specific activity. It is established that the fibers obtained by using catalase of microbiological origin possess high stability and their activity does not practically change in the aqueous environment. The unpurified catalase is one and a half higher than at purified catalase. Under laboratory conditions there turned out the experimental batches of fibers and there conducted their endurance tests. Catalase included in cellulase triacetate has effectively functioned during a period of 2 years purifying the distilled water containing 50 mg/l of hydrogen peroxide.