Fe3O4 particles coated with acrylic copolymer (ACP) of about 5--8 nm in diameter were synthesized and used for immobilization of horseradish peroxidase (HRP). Direct electrochemistry of HRP embedded in the nanosized F...Fe3O4 particles coated with acrylic copolymer (ACP) of about 5--8 nm in diameter were synthesized and used for immobilization of horseradish peroxidase (HRP). Direct electrochemistry of HRP embedded in the nanosized Fe304 solid matrix modified paraffin impregnated graphite electrode (PIGE) was achieved,which is related to the heine Fe(Ⅲ)/Fe(Ⅱ) conversion of HRP. Cyclic voltammetry gave a pair of reproducible and welldefined redox peaks at about Ea of -0.295 V vs. SCE. The standard rate constant k, was determined as 2.7 s^-1. It demonstrated that the nano-Fe3O4 solid matrix offers a friendly platform to assemble the HRP protein molecules and enhance the electron transfer rate between the HRP and the electrode. UV-Vis absorption spectra and WrIR spectra studies revealed that the embedded HRP retained its native-like structure. The HRP/Fe3O4/PIGE showed a strong catalytic activity toward H2O2. The voltammetric response was a linear function of H2O2 concentration in the range of 10-140μmol/L with detection limit of 7.3 μmol/L (s/n = 3 ). The apparent Michaelis-Menten constant is calculated to be 0.42 mmol/L.展开更多
基金Project supported by the University of Science and Technology of China(Nos.ky1212 and ky2216).
文摘Fe3O4 particles coated with acrylic copolymer (ACP) of about 5--8 nm in diameter were synthesized and used for immobilization of horseradish peroxidase (HRP). Direct electrochemistry of HRP embedded in the nanosized Fe304 solid matrix modified paraffin impregnated graphite electrode (PIGE) was achieved,which is related to the heine Fe(Ⅲ)/Fe(Ⅱ) conversion of HRP. Cyclic voltammetry gave a pair of reproducible and welldefined redox peaks at about Ea of -0.295 V vs. SCE. The standard rate constant k, was determined as 2.7 s^-1. It demonstrated that the nano-Fe3O4 solid matrix offers a friendly platform to assemble the HRP protein molecules and enhance the electron transfer rate between the HRP and the electrode. UV-Vis absorption spectra and WrIR spectra studies revealed that the embedded HRP retained its native-like structure. The HRP/Fe3O4/PIGE showed a strong catalytic activity toward H2O2. The voltammetric response was a linear function of H2O2 concentration in the range of 10-140μmol/L with detection limit of 7.3 μmol/L (s/n = 3 ). The apparent Michaelis-Menten constant is calculated to be 0.42 mmol/L.
