NDLI: A novel acetylcholinesterase biosensor based on carboxylic graphene coated with silver nanoparticles for pesticide detection.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Liu, Yongjun Wang, Guangcan Li, Canpeng Zhou, Qing Wang, Min Yang, Long
Description	Country affiliation: China Author Affiliation: Liu Y ( School of Chemical Science and Engineering, Yunnan University, Kunming 650091, China.); Wang G ( School of Chemical Science and Engineering, Yunnan University, Kunming 650091, China. Electronic address: wangc166163@sina.com.); Li C ( School of Chemical Science and Engineering, Yunnan University, Kunming 650091, China.); Zhou Q ( School of Physical Science and Technology, Yunnan University, Kunming 650091, China.); Wang M ( School of Chemical Science and Engineering, Yunnan University, Kunming 650091, China.); Yang L ( School of Chemical Science and Engineering, Yunnan University, Kunming 650091, China.)
Abstract	A novel acetylcholinesterase (AChE) biosensor based on Ag NPs, carboxylic graphene (CGR) and Nafion (NF) hybrid modified glass carbon electrode (GCE) has been successfully developed. Ag NPs-CGR-NF possessed predominant conductivity, catalysis and biocompatibility and provided a hydrophilic surface for AChE adhesion. Chitosan (CS) was used to immobilize AChE on the surface of Ag NPs-CGR-NF/GCE to keep the AChE activities. The AChE biosensor showed favorable affinity to acetylthiocholine chloride (ATCl) and could catalyze the hydrolysis of ATCl with an apparent Michaelis-Menten constant value of 133 µM, which was then oxidized to produce a detectable and fast response. Under optimum conditions, the biosensor detected chlorpyrifos and carbaryl at concentrations ranging from 1.0×10(-13) to 1×10(-8) M and from 1.0×10(-12) to 1×10(-8) M. The detection limits for chlorpyrifos and carbaryl were 5.3×10(-14) M and 5.45×10(-13) M, respectively. The developed biosensor exhibited good sensitivity, stability, reproducibility and low cost, thus providing a promising tool for analysis of enzyme inhibitors. This study could provide a simple and effective immobilization platform for meeting the demand of the effective immobilization enzyme on the electrode surface.
File Format	HTM / HTML
ISSN	09284931
Volume Number	35
e-ISSN	18730191
Journal	Materials Science and Engineering: C
Language	English
Publisher	Elsevier
Publisher Date	2014-02-01
Publisher Place	Netherlands
Access Restriction	Subscribed
Subject Keyword	Discipline Materials Science Acetylcholinesterase Chemistry Biosensing Techniques Instrumentation Conductometry Graphite Nanoparticles Pesticides Analysis Silver Adsorption Carboxylic Acids Cholinesterase Inhibitors Electrodes Equipment Design Equipment Failure Analysis Ultrastructure Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Mechanics of Materials Biomaterials Condensed Matter Physics Bioengineering Mechanical Engineering

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