Abstract
Loss in activity remains key challenges for the potential use of laccase in industrial and environmental biotechnology. Enzyme immobilization is an exciting alternative for improving the stability and reusability of enzymatic processes. In this study, the laccase enzyme was successfully immobilized onto SiO2 supports through covalent binding. The stability and durability during the reuse of immobilized laccase were superior to free laccase. After 30 reaction cycles of continuous use, the relative activity was above 80%. In addition, immobilized laccase was able to degrade Bisphenol A (BPA) more effectively than free laccase, especially in the presence of TX-100. The BPA was completely degraded within an incubation time of 5h. The results suggest that immobilization is feasible for improving the stability and reusability of laccase for many applications.
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