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Synergistic stabilization of laccase within a Co-malonate framework: Characterization and its biocatalytic application in BPA degradation

Aug 2026 · Inorganic and Nano-Metal Chemistry · Vol 56, pp. 849 - 860 · 0 citations · 63 references

Abstract

Abstract In this study, a hybrid biocatalyst was developed via rapid in-situ biomineralization of laccase within a cobalt(II)-malonate framework (Lac@MOF). The novelty lies in using malonic acid as a biocompatible linker, enabling rapid enzyme encapsulation under mild conditions. Structural integrity was confirmed through SEM, TGA, EDS, and XPS analyses. Lac@MOF exhibited expanded operational pH and temperature ranges. A notable enhancement in catalytic activity (∼150%) was observed at elevated temperatures, suggesting that the framework stabilizes the enzyme’s active conformation against thermal denaturation. The hybrid material achieved ∼66% Bisphenol A (BPA) removal within 240 min and retained 60% of its initial activity after seven reuse cycles. These findings demonstrate that the Co-malonate framework effectively enhances laccase stability and reusability. The developed biocomposite offers a cost-effective and robust strategy for industrial scale-up, providing a promising platform for the efficient biocatalytic treatment of endocrine-disrupting micro-pollutants in environmental remediation.

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