Direct electrochemistry and electrocatalysis of horseradish peroxidase immobilized on L-glutathione

来源 :Chinese Chemical Letters | 被引量 : 0次 | 上传用户:linshenxiu
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A novel hydrogen peroxide biosensor has been fabricated based on covalently linked horseradish peroxidase(HRP)onto L- glutathione self-assembled monolayers(SAMs).The SAMs-based electrode was characterized by electrochemical methods,and direct electrochemistry of HRP can be achieved with formal potential of-0.242 V(vs.saturated Ag/AgCl)in pH 7 phosphate buffer solution(PBS),the redox peak current is linear to scan rate and rate constant can be calculated to be 0.042s~(-1).The HRP-SAMs- based biosensors show its better electrocatalysis to hydrogen peroxide in the concentration range of 1×10~(-6)mol/L to 1.2×10~(-3)mol/L with a detection limit of 4×10~(-7)mol/L.The apparent Michealis-Menten constant is 3.12 mmol/L.The biosensor can effectively eliminate the interferences of dopamine,ascorbic acid,uric acid,catechol and p-acetaminophen. A novel hydrogen peroxide biosensor has been fabricated based on covalently linked horseradish peroxidase (HRP) onto L- glutathione self-assembled monolayers (SAMs). The SAMs-based electrode was characterized by electrochemical methods, and direct electrochemistry of HRP can be achieved with formal potential of-0.242 V (vs.saturated Ag / AgCl) in pH 7 phosphate buffer solution (PBS), the redox peak current is linear to scan rate and rate constant can be calculated to be 0.042 s -1. The HRP -SAMs-based biosensors show its better electrocatalysis to hydrogen peroxide in the concentration range of 1 × 10 -6 mol / L to 1.2 × 10 -3 mol / L with a detection limit of 4 × 10 ~ (- -7) mol / L.The apparent Micheal-Menten constant is 3.12 mmol / L.The biosensor can effectively eliminate the interferences of dopamine, ascorbic acid, uric acid, catechol and p-acetaminophen.
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