Immobilisation of catalase purified from mushroom (Hydnum repandum) onto glutaraldehyde-activated chitosan and characterisation: Its application for the removal of hydrogen peroxide from artificial wastewater

Abstract

Hydrogen peroxide (H2O2) is a chemical that is widely used in many industrial processes, and, except at certain concentrations, it is toxic in biological systems such as water and air. Among enzymes, catalases are important industrial enzymes because of their role in the conversion of hydrogen peroxide to water and molecular oxygen. Herein, catalase (CAT) from Hydnum repandum was purified 3.02-fold with a yield of 68.10% by three-phase partitioning (TPP) for the first time. The purified catalase was immobilised on glutaraldehyde-activated chitosan (Glu-Cts), and its applicability for the removal of hydrogen peroxide released from industrial processes was investigated. The results of the present study showed that the optimum pH and temperature were found to be 7.0 and 30°C for both free and immobilised catalase (CAT-Glu-Cts). The catalytic efficiency (V max/K m) of the immobilised enzyme increased 8-fold compared to the free enzyme. CAT-Glu-Cts was shown to have better pH, thermal stability, and storage stability than free CAT. In this study, >96% of 6 mM, 15 ve 24 mM H2O2 was removed from artificial wastewater after 2 h using immobilised catalase. We expect that CAT-Glu-Cts, obtained by purifying a plant-derived catalase and immobilising it into an environmentally friendly and biocompatible material, is a promising candidate that can be safely used for H2O2 removal in various branches of industry.

Keywords

• catalase
• three-phase partitioning
• immobilisation
• characterisation
• h2o2 removal