Horseradish peroxidase-catalyzed polymerization of L-DOPA for mono-/bi-enzyme immobilization and amperometric biosensing of H2O2 and uric acid
Horseradish peroxidase-catalyzed polymerization of L-DOPA for mono-/bi-enzyme immobilization and amperometric biosensing of H2O2 and uric acid
复制标题
辣根过氧化物酶催化的 L-DOPA 聚合用于单酶/双酶固定以及 H2O2 和尿酸的电流生物传感
DOI:
10.1016/j.talanta.2015.11.047
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发表时间:
2016-03-01
期刊:
影响因子:
6.1
通讯作者:
Meng, Wenhua
中科院分区:
文献类型:
--
作者:
Dai, Mengzhen;Huang, Ting;Meng, Wenhua
Horseradish peroxidase (HRP)-catalyzed polymerization of L-DOPA (vs. dopamine) in the presence of H2O2 (and uricase (UOx)) was exploited to immobilize mono-/bi-enzymes for hydroquinone-mediated amperometric biosensing of H2O2 and uric acid (UA). The relevant polymeric biocomposites (PBCs) were prepared in phosphate buffer solution containing HRP and L-DOPA (or plus UOx) after adding H2O2. The mono-/bi-enzyme amperometric biosensors were prepared simply by casting some of the PBCs on Au plated Au (Au-plate/Au) electrodes, followed by coating with an outer-layer chitosan (CS) film for each. UV-vis spectrophotometry, scanning electron microscopy, cyclic voltammetry and electrochemical impedance spectroscopy were used for film characterization and/or process monitoring. The HRP immobilized by enzyme catalysis well preserved its bioactivity, as confirmed by UV-vis spectrophotometry. Under optimized conditions, the monoenzyme CS/HRP-poly(L-DOPA) (PD)/Au-plate/Au electrode potentiostated at -0.1 V responded linearly to H2O2 concentration from 0.001 to 1.25 mM with a sensitivity of 700 mu A mM(-1) cm(-2) and a limit of detection (LOD) of 0.1 mu M, and the bienzyme CS/UOx-HRP-PD/Au-plate/Au electrode at 0.1 V responded linearly to UA concentration from 0.001 to 0.4 mM with a sensitivity of 349 mu A mM(-1) cm(-2) and a LOD of 0.1 mu M. The mono-/bi-enzyme biosensors based on biosynthesized PD performed better than many reported analogues and those based on similarly biosynthesized polydopamine. (C) 2015 Elsevier B.V. All rights reserved.