Peroxidase-like activity of apoferritin paired gold clusters for glucose detection

Xin Jiang; Cuiji Sun; Yi Guo; Guangjun Nie; Li Xu

doi:10.1016/j.bios.2014.08.078

Peroxidase-like activity of apoferritin paired gold clusters for glucose detection

Xin Jiang, Cuiji Sun, Yi Guo, Guangjun Nie, Li Xu

Research output: Contribution to journal › Article › peer-review

138 Scopus citations

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 K_m value (0.097mM) and a higher K_cat 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)
Pages (from-to)	165-170
Number of pages	6
Journal	Biosensors and Bioelectronics
Volume	64
DOIs	https://doi.org/10.1016/j.bios.2014.08.078
State	Published - Feb 15 2015

Keywords

Apoferritin
Glucose
Gold clusters
Kinetic study
Peroxidase-like activity

ASJC Scopus subject areas

Biophysics
Biomedical Engineering
Biotechnology
Electrochemistry

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10.1016/j.bios.2014.08.078

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@article{cc2d39ef90ed41c1b5eb20080c83b4c2,

title = "Peroxidase-like activity of apoferritin paired gold clusters for glucose detection",

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.",

keywords = "Apoferritin, Glucose, Gold clusters, Kinetic study, Peroxidase-like activity",

author = "Xin Jiang and Cuiji Sun and Yi Guo and Guangjun Nie and Li Xu",

note = "Funding Information: The work was supported by the National Natural Science Foundation of China (No. 81271697 ), the Specialized Research Fund for the Doctoral Program of Higher Education of China (Nos. 20100061120077 , 20120061110021 ), the Social Development Project of Science and Technology Department of Jilin Province, China (Nos. 20106031 , 20120967 , YYZX201264 , 20130206069GX ), the Fundamental Research Funds for the Central Universities , and “Significant New Drug Creation” Science and Technology Major Program (No. 2012ZX09503001-003 ). Publisher Copyright: {\textcopyright} 2014 Elsevier B.V. Copyright: Copyright 2019 Elsevier B.V., All rights reserved.",

year = "2015",

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doi = "10.1016/j.bios.2014.08.078",

language = "English (US)",

volume = "64",

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AU - Jiang, Xin

AU - Sun, Cuiji

AU - Guo, Yi

AU - Nie, Guangjun

AU - Xu, Li

N1 - Funding Information: The work was supported by the National Natural Science Foundation of China (No. 81271697 ), the Specialized Research Fund for the Doctoral Program of Higher Education of China (Nos. 20100061120077 , 20120061110021 ), the Social Development Project of Science and Technology Department of Jilin Province, China (Nos. 20106031 , 20120967 , YYZX201264 , 20130206069GX ), the Fundamental Research Funds for the Central Universities , and “Significant New Drug Creation” Science and Technology Major Program (No. 2012ZX09503001-003 ). Publisher Copyright: © 2014 Elsevier B.V. Copyright: Copyright 2019 Elsevier B.V., All rights reserved.

PY - 2015/2/15

Y1 - 2015/2/15

N2 - 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.

AB - 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.

KW - Apoferritin

KW - Glucose

KW - Gold clusters

KW - Kinetic study

KW - Peroxidase-like activity

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ER -

Peroxidase-like activity of apoferritin paired gold clusters for glucose detection

Abstract

Keywords

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