The present work describes the results of the preliminary characterization of a novel enzyme with catalase activity isolated from psychrotolerant bacteria. Catalases decompose hydrogen peroxide (H2O2) to water and oxygen. Chemical immobilization is the best solution in case of reactions in which a gaseous product is created hence immobilization via divinyl sulfone having used a polymeric regenerated cellulose membrane was proposed. The preparations were checked according to their activity and stability. In the textile industry, a catalase is used to decompose the hydrogen peroxide waste after bleaching fabrics. During photocatalytic oxidation, H2O2 is added at relatively high concentration app. 20-80 g/L and the pH of these solutions is in the range between 7 and 10. The psychrophilic catalase described in this work presents high activity up to 40 g/L at pH 7-10, while a commercial alternative isolated from bovine liver only displays activity up to 14 g/L at pH not higher than 9. The stability of enzymatic activity is strongly dependent on temperature and is also a function of substrate concentration. The results obtained with this psychrophilic catalase are promising for textile effluence treatment.