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

Peroxidase-like activity of apoferritin paired gold clusters for glucose detection
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DOI:
10.1016/j.bios.2014.08.078
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发表时间:
2015-02-15
影响因子:
12.6
通讯作者:
Xu, Li
Xu, Li
中科院分区:
工程技术1区
文献类型:
--
作者:
Jiang, Xin;Sun, Cuiji;Xu, Li

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贵金属纳米团簇的发现和应用受到了人们的极大关注。本文报道了载铁蛋白配对金团簇(Au-Ft)能有效地催化H_2O_2氧化3.3‘,5.5’-四甲基联苯胺(TMB)而产生蓝色反应。与天然酶相比,Au-Ft在酸性pH附近表现出较高的活性,并且可以在较宽的温度范围内使用。载脂蛋白纳米笼增强底物TMB与H_2O_2的反应活性。Au-Ft催化的反应符合典型的Michaelis-Menten动力学。与辣根过氧化物酶相比,TMB的K-m值(0.097 mm)较低,K-CAT值(5.80×10~(4)S(-1))较高。基于这些发现,Au-Ft作为过氧化物酶的模拟物,对葡萄糖进行了酶促分光光度分析。该体系具有较好的重复性和较高的生物选择性,具有广阔的应用前景。(C)2014爱思唯尔B.V.保留所有权利。
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 (0.097 mM) and a higher K-cat value (5.8 x 10(4) s(-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. (C) 2014 Elsevier B.V. All rights reserved.