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.
Hydrogen peroxide (H2O2) is widely used in industrial and environmental processes; however, excessive accumulation of H2O2 may cause oxidative damage and environmental hazards. Catalase (CAT) is an efficient enzyme capable of decomposing H2O2 into water and oxygen, but its practical application is limited by low stabil...
Ceyhun Işık, Özgün Vatansever, M. Teke· RSC Advances· 0 citations
Laccase provides a green and eco-friendly solution for the degradation of widely used anthraquinone and triphenylmethane dyes. However, its practical application remains constrained by several obstacles, including poor stability, low redox potential, and mediator leakage, which affect both dye degradation efficiency an...
Jiao Yu, Sheng-Long Liu, Yi-Meng Teng et al.· Journal of Hazardous Materia...· 0 citations
The practical implementation of enzyme bioelectrodes is limited by the inherent lability of proteins, which require mild conditions to maintain both catalytic activity and long‐term stability. The lack of standardized reference parameters and the inherent complexity of biointerfaces also hinder direct comparison amon...
W. García-García, G. Huerta-Miranda, K. Juárez et al.· Electroanalysis· 0 citations
The degradation of perfluorooctanoic acid (PFOA) remained challenging due to the extraordinary stability of its carbon–fluorine bonds, which were resistant to conventional photocatalytic processes. In this work, a metal–organic framework (MOF), MIL-125-NH2, was grown in situ on reduced graphene oxide (rGO) to form na...
Laccases are multicopper oxidases capable of oxidizing a wide range of substrates using molecular oxygen as the terminal electron acceptor, producing water as the sole by-product. High-redox potential fungal laccases, such as those from Trametes versicolor, are particularly attractive for industrial and environmental a...
Jessica Costa, A. Atrei, J. J. Valle-Delgado et al.· Biomolecules· 0 citations
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