Abstract
The discovery and application of noble metal nanoclusters have received considerable attention. In this paper, we reported that apoferritin paired gold clusters (Au-Ft) could efficiently catalyze oxidation of 3.3',5.5'-tetramethylbenzidine (TMB) by H2O2 to produce a blue color reaction. Compared with natural enzyme, Au-Ft exhibited higher activity near acidic pH and could be used over a wide range of temperatures. Apoferritin nanocage enhanced the reaction activity of substrate TMB by H2O2. The reaction catalyzed by Au-Ft was found to follow a typical Michaelis-Menten kinetics. The kinetic parameters exhibited a lower Km value (0.097mM) and a higher Kcat value (5.8×104s-1) for TMB than that of horse radish peroxidase (HRP). Base on these findings, Au-Ft, acting as a peroxidase mimetic, performed enzymatic spectrophotometric analysis of glucose. This system exhibited acceptable reproducibility and high selectivity in biosening, suggesting that it could have promising applications in the future.
Original language | English (US) |
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Pages (from-to) | 165-170 |
Number of pages | 6 |
Journal | Biosensors and Bioelectronics |
Volume | 64 |
DOIs | |
State | Published - Feb 15 2015 |
Keywords
- Apoferritin
- Glucose
- Gold clusters
- Kinetic study
- Peroxidase-like activity
ASJC Scopus subject areas
- Biophysics
- Biomedical Engineering
- Biotechnology
- Electrochemistry