• Journal of Microbiology and Biotechnology
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• v.17 no.6
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• pp.960-967
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• 2007

The co-immobilization of Aspergillus niger glucose oxidase (GOD) with bovine liver catalase (CAT) onto florisil (magnesium silicate-based porous carrier) was investigated to improve the catalytic efficiency of GOD against $H_2O2$ inactivation. The effect of the amount of bound CAT on the GOD activity was also studied for 12 different initial combinations of GOD and CAT, using simultaneous and sequential coupling. The sequentially co-immobilized GOD-CAT showed a higher efficiency than the simultaneously co-immobilized GOD-CAT in terms of the GOD activity and economic costs. The highest activity was shown by the sequentially co-immobilized GOD-CAT when the initial amounts of GOD and CAT were 10 mg and 5 mg per gram of carrier. The optimum pH, buffer concentration, and temperature for GOD activity for the same co-immobilized GOD-CAT sample were then determined as pH 6.5, 50 mM, and $30^{\circ}C$, respectively. When compared with the individually immobilized GOD, the catalytic activity of the co-immobilized GOD-CAT was 70% higher, plus the reusability was more than two-fold. The storage stability of the co-immobilized GOD-CAT was also found to be higher than that of the free form at both $5^{\circ}C\;and\;25^{\circ}C$. The increased GOD activity and reusability resulting from the co-immobilization process may have been due to CAT protecting GOD from inactivation by $H_2O2$ and supplying additional $O_2$ to the reaction system.

• Korean Chemical Engineering Research
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• v.61 no.4
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• pp.576-583
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• 2023

This study aimed to investigate the impact of enhancing the electrode conductivity and mitigating the production of hydrogen peroxide - a by-product arising from lactate oxidation - on the performance of lactate electrodes. The electrical conductivity of the electrode was improved by modifying the surface of carbon paper with single-walled carbon nanotubes. Catalase was introduced to effectively eliminate the hydrogen peroxide produced during the lactate oxidation reaction. The carbon paper electrode, with simultaneous immobilization of both lactate oxidase and catalase, yielded a current 1.7 times greater than the electrode where only lactate oxidase was immobilized. The electrode in which lactate oxidase and catalase were co-immobilized on the surface of carbon paper modified with single-walled carbon nanotubes, produced a current of 171 µA, which was more than twice as much current as the carbon paper with only lactate oxidase immobilized. The optimized electrode showed a linear response up to lactate concentration of 20 mM, confirming that it can be used as a sensor electrode.