Journal
BIOSENSORS & BIOELECTRONICS
Volume 30, Issue 1, Pages 43-48Publisher
ELSEVIER ADVANCED TECHNOLOGY
DOI: 10.1016/j.bios.2011.08.024
Keywords
His-tag affinity immobilization; Nickel nanoparticles; Acetylcholinesterase biosensor; Pesticides
Categories
Funding
- National Science Foundation [0727861, 0954919]
- Direct For Mathematical & Physical Scien
- Division Of Materials Research [0954919] Funding Source: National Science Foundation
- Office Of The Director
- Office Of Internatl Science &Engineering [0727861] Funding Source: National Science Foundation
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This paper reports site-specific affinity immobilization of(His)6-tagged acetylcholinesterase (AChE) onto Ni/NiO nanoparticles for the development of an electrochemical screen-printed biosensor for the detection of organophosphate pesticides. The method is based on the specific affinity binding of the His-tagged enzyme to oxidized nickel nanoparticle surfaces in the absence of metal chelators. This approach allows stable and oriented attachment of the enzyme onto the oxidized nickel through the external His residue in one-step procedure, allowing for fast and sensitive detection of paraoxon in the concentration range from 10(-8) to 10(-13) M. A detection limit of 10(-12) M for paraoxon was obtained after 20 min incubation. This method can be used as a generic approach for the immobilization of other His-tagged enzymes for the development of biosensors. (C) 2011 Elsevier B.V. All rights reserved.
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