Abstract
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. 20–80g/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 40g/L at pH 7–10, while a commercial alternative isolated from bovine liver only displays activity up to 14g/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.
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