标题:Direct electrochemistry of glucose oxidase immobilized on nanostructured gold thin films and its application to bioelectrochemical glucose sensor
作者:Qiu, Cuicui; Wang, Xia; Liu, Xueying; Hou, Shifeng; Ma, Houyi
作者机构:[Qiu, Cuicui; Ma, Houyi] Shandong Univ, Sch Chem & Chem Engn, State Educ Minist, Key Lab Colloid & Interface Chem, Jinan 250100, Peoples R China.; [ 更多
通讯作者:Ma, H
通讯作者地址:[Ma, HY]Shandong Univ, Sch Chem & Chem Engn, State Educ Minist, Key Lab Colloid & Interface Chem, Jinan 250100, Peoples R China.
来源:ELECTROCHIMICA ACTA
出版年:2012
卷:67
页码:140-146
DOI:10.1016/j.electacta.2012.02.011
关键词:Glucose oxidase (GOx); Electron transfer; Bioelectrochemical sensor;; Gold film; Electrochemical detection
摘要:Glucose oxidase (GOx) was stably immobilized via a simple physical adsorption method onto the nanostructured Au thin films fabricated by using electrodeposition and galvanic replacement technology, which provides a facile method to prepare morphology-controllable Au films and also facilitates the preparation and application of enzyme modified electrodes. An obvious advantage of the as-prepared enzyme electrode (denoted as GOx/Au/GCE) is that the nano-Au films provide a favorable microenvironment for GOx and facilitate the electron transfer between the active center of GOx and electrodes. Cyclic voltammetry (CV) results indicate that the immobilized GOx displayed a direct, reversible and surface-confined redox reaction in the phosphate buffer solution. Furthermore, the enzyme modified electrode was used as a glucose bioelectrochemical sensor, exhibiting a linear relationship in the concentration ranges of 2.5-32.5 mu mol L-1 and 60-130 mu mol L-1 with a detection limit of 0.32 mu mol L-1 (S/N = 3) at an applied potential of -0.55 V. Due to the excellent stability, sensitivity and anti-interference ability, the Au thin films are hopeful in the construction of glucose biosensors. (C) 2012 Elsevier Ltd. All rights reserved.
收录类别:EI;SCOPUS;SCIE
WOS核心被引频次:46
Scopus被引频次:50
资源类型:期刊论文
原文链接:https://www.scopus.com/inward/record.uri?eid=2-s2.0-84862800580&doi=10.1016%2fj.electacta.2012.02.011&partnerID=40&md5=372fc763db9b7e1617a490a86f0c6871
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