Abstract
Metal-organic frameworks(MOFs) have been widely regarded as promising carriers for enzyme immobilization owing to their advantages in improving loading and regulating interaction with enzymes. However, they are still suffering from the problems of slow mass transfer and compromising activity. In this paper, the active two-dimensional(2D) MOF of Cu-TCPP(Fe)[TCPP=tetrakis(4-carboxy-phenyl)porphyrin], which possesses the biomimetic architecture of peroxidase, was adopted to anchor cytochrome(Cyt c) for the enhancement of catalytic activity. The atomic/nanometer thickness and micrometer lateral dimension of 2D MOFs can ensure the full exposure of immobilized enzymes and a shorter diffusion distance for the reactant molecules. Besides, the active carrier can provide synergistic catalysis and activity compensation during the reaction. When tested in the decomposition reaction of H2O2, Cyt c/Cu-TCPP(Fe) exhibited nearly twice catalytic activity and an accelerated catalytic rate compared to free Cyt c.
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This work was supported by the National Natural Science Foundation of China (Nos.21908105 and 21971114) and the Fund of Nanjing Municipal Science and Technology Innovation Project, China.
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Synergistic catalysis of enzymes and biomimetic MOFs: immobilizing Cyt c on two-dimensional MOFs to enhance the performance of peroxidase
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Wang, Y., Meng, F., Su, R. et al. Synergistic Catalysis of Enzymes and Biomimetic MOFs: Immobilizing Cyt c on Two-dimensional MOFs to Enhance the Performance of Peroxidase. Chem. Res. Chin. Univ. 38, 1356–1360 (2022). https://doi.org/10.1007/s40242-022-2257-9
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DOI: https://doi.org/10.1007/s40242-022-2257-9