Please use this identifier to cite or link to this item: http://dx.doi.org/10.18419/opus-845
Authors: Schulze, Holger
Vorlová, Sandra
Villatte, Francois
Bachmann, Till T.
Schmid, Rolf D.
Title: Design of acetylcholinesterases for biosensor applications
Issue Date: 2003
metadata.ubs.publikation.typ: Preprint
metadata.ubs.publikation.source: Biosensors & bioelectronics 18 (2003), S. 201-209. URL http://dx.doi.org/10.1016/S0956-5663(02)00184-7
URI: http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-26945
http://elib.uni-stuttgart.de/handle/11682/862
http://dx.doi.org/10.18419/opus-845
Abstract: In recent years, the use of acetylcholinesterases (AChEs) in biosensor technology has gained enormous attention, in particular with respect to insecticide detection. The principle of biosensors using AChE as a biological recognition element is based on the inhibition of the enzyme’s natural catalytic activity by the agent that is to be detected. The advanced understanding of the structure-function-relationship of AChEs serves as the basis for developing enzyme variants, which, compared to the wild type, show an increased inhibition efficiency at low insecticide concentrations and thus a higher sensitivity. This review describes different expression systems that have been used for the production of recombinant AChE. In addition, approaches to purify recombinant AChEs to a degree that is suitable for analytical applications will be elucidated as well as the various attempts that have been undertaken to increase the sensitivity of AChE to specified organophosphates and carbamates using side-directed mutagenesis and employing the enzyme in different assay formats.
Appears in Collections:03 Fakultät Chemie

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