Protein-Metal Organic Framework Hybrid Composites with Intrinsic Peroxidase-like Activity as a Colorimetric Biosensing Platform

Artificial enzyme mimetics have received considerable attention because natural enzymes have some significant drawbacks, including enzyme autolysis, low catalytic activity, poor recovery, and low stability to environmental changes. Herein, we demonstrated a facile approach for one pot synthesis of hemeprotein-metal organic framework hybrid composites (H-MOFs) by using bovine hemoglobin (BHb) and zeolitic imidazolate framework-8 (ZIF-8) as a model reaction system. Surprisingly, the new hybrid composites exhibit 423% increase in peroxidase-like catalytic activity compared to free BHb. Taking advantages of the unique pore structure of H-MOFs with high catalytic property, a H-MOFs-based colorimetric biosensing platform was newly constructed and applied for the fast and sensitive detection of hydrogen peroxide (H2O2) and phenol. The corresponding detection limits as low as 1.0 mu M for each analyte with wide linear ranges (0-800 mu M for H2O2 and 0-200 mu M for phenol) were obtained by naked-eye visualization. Significantly, a sensitive and selective method for visual assay of trace H2O2 in cells and phenol in sewage was achieved with this platform. The stability of H-MOFs was also examined, and excellent reproducibility and recyclability without losing in their activity were observed. In addition, the general applicability of H-MOFs was also investigated by using other hemeproteins (horseradish peroxidase, and myoglobin), and the corresponding catalytic activities were 291% and 273% enhancement, respectively. This present work not only expands the application of MOFs but also provides an alternative technique for biological and environmental sample assay.