[Immobilized catalase in water purification systems]

Area of Science:

• Biocatalysis
• Biotechnology
• Materials Science

Background:

• Enzyme immobilization is crucial for biocatalyst stability and reusability.
• Cellulose triacetate offers a promising matrix for enzyme immobilization.
• Penicillium fungus is a viable source for catalase production.

Purpose of the Study:

• To develop a stable biocatalyst based on catalase immobilized in cellulose triacetate fibers.
• To evaluate the enzymatic activity and stability of the immobilized catalase.
• To assess the performance of the biocatalyst in water purification.

Main Methods:

• Catalase production from Penicillium fungus using ethyl alcohol precipitation.
• Enzyme concentration via vacuum-rotor evaporation.
• Immobilization of catalase within cellulose triacetate fibers during formation.
• Comparative analysis of different polymers (cellulose triacetate, chlorine, polysulphone) for immobilization.
• Stability and endurance testing of the biocatalyst in aqueous environments.

Main Results:

• Cellulose triacetate fibers exhibited the highest enzymatic activity for immobilized catalase.
• Fine biocatalyst fibers showed higher specific activity.
• Immobilized catalase demonstrated high stability in aqueous environments, with unpurified catalase showing 1.5x higher activity than purified.
• The biocatalyst effectively purified distilled water containing 50 mg/l hydrogen peroxide over a 2-year period.

Conclusions:

• Catalase immobilized in cellulose triacetate fibers provides a stable and effective biocatalyst.
• Microbiological catalase immobilized in fibers exhibits excellent stability and performance in water purification.
• This biocatalyst shows potential for long-term application in water treatment processes.