Immobilization of peroxidase onto the surface of degradable starch moiety aggregates as a way to change their surface properties excerpts from English literature translationImmobilisation of catalase

H stability of the immobilized catalase were evaluated by measuring the enzyme activity before and after immobilization, and by determining the optimal pH range of the immobilized enzyme.

2.2.2. CNBr activation and immobilization method

SCA and SPCL discs (~3.0g) were activated by immersion in 100 mM CNBr solution in 70% (v/v) formic acid for 30 min at 0°C. The discs were then washed with 2% (w/v) NaHCO3 solution, followed by distilled water. The activated discs were then immersed in 20 mL of the enzyme solution (358U/g support and 19 mg protein/g support) by way of diluting 10 times the original enzyme solution with a universal buffer (pH 3-12) for 19 h at room temperature. After the desired contact time, the residual enzyme was filtered and the support was washed with the same buffer.

3. Results and discussion

The surface of SCA and SPCL discs was modified by the immobilization of catalase using two different methods. The effectiveness of the immobilization methods was evaluated in terms of the activity and stability of the immobilized catalase.

The epichlorohydrin treatment method resulted in higher immobilization efficiency and higher retention of enzyme activity than the CNBr activation method. The immobilized catalase showed good stability at different pH values, retaining more than 90% of its activity at pH 5-10.

Overall, the immobilization of catalase onto the surface of biodegradable starch-based polymers can change their surface properties and enhance their stability. This approach has potential applications in various fields, including biocatalysis, biomedicine, and environmental science