Abstract

In this paper, N, Fe-codoped carbon dots (N, Fe-CDs) were synthesized from β-cyclodextrin, ethylenediamine, and ferric chloride for the first time using a convenient one-step hydrothermal method. The obtained N, Fe-CDs were characterized by various methods including transmission electron microscopy, X-ray photoelectron spectroscopy, and Fourier-transform infrared spectroscopy. The N, Fe-CDs exhibited better catalytic activity than horseradish peroxidase (HRP) and caused an evident color change for 3,3′,5,5′-tetramethylbenzidine in the presence of H2O2. Kinetic experiments show that the apparent Km value for the N, Fe-CDs with TMB (0.40 mM) or H2O2 (0.35 mM) as the substrate was lower than that of HRP (0.43 and 3.70 mM), suggesting that the N, Fe-CDs have a much higher affinity for TMB and H2O2 than HRP. The Km/Vmax value for the N, Fe-CDs (21.74×103·s for H2O2) is significantly lower than that for HRP (42.53×103·s), suggesting that the N, Fe-CDs have a stronger catalytic efficiency for H2O2 than HRP. Furthermore, a highly efficient and sensitive colorimetric detection method for glucose was developed using the N, Fe-CDs as mimic peroxidase to detect the hydrogen peroxide generated by the oxidation of glucose by glucose oxidase. The limit of detection for H2O2 and glucose was found to be 0.52 and 3.0 μM, respectively. The obtained N, Fe-codoped carbon dots, which possess simulated peroxidase activity, can potentially be used in the field of biotechnology.

Highlights

  • Peroxidase such as horseradish peroxidase (HRP) is a kind of natural enzyme that catalyzes the decomposition of peroxides and prevents biological cells from being damaged by toxic substances [1]

  • The results indicate that catalytic activity of the N, FeCDs was highest at a pH of 2.5

  • N, Fe-CDs were synthesized from β-cyclodextrin, ethylenediamine, and FeCl3∙6H2O using a one-step hydrothermal method for the first time

Read more

Summary

Introduction

Peroxidase such as horseradish peroxidase (HRP) is a kind of natural enzyme that catalyzes the decomposition of peroxides and prevents biological cells from being damaged by toxic substances [1].

Methods
Results
Conclusion
Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call