1 research outputs found
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 (H<sub>2</sub>O<sub>2</sub>) and phenol. The corresponding detection limits as
low as 1.0 μM for each analyte with wide linear ranges (0–800
μM for H<sub>2</sub>O<sub>2</sub> and 0–200 μM
for phenol) were obtained by naked-eye visualization. Significantly,
a sensitive and selective method for visual assay of trace H<sub>2</sub>O<sub>2</sub> 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