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- W2317323979 endingPage "5277" @default.
- W2317323979 startingPage "5270" @default.
- W2317323979 abstract "Since all of the organophosphorus pesticides (OPP) inhibit the cholinesterases with a common mechanism, it is still challenging to detect OPP selectively with inhibition-based biosensors. This study focuses on the conversion of a typical inhibition biosensing to a selective substrate-like biosensing. The interaction of quinalphos with plant-esterase involves not only a decrease in enzyme activity but also a heterolytic bond cleavage of quinalphos. The leaving group eliminated from quinalphos is an ideal biomarker due to its specificity in most OPP. Thus, using 2-hydroxyquinoxaline (HQO), the leaving group of quinalphos, as the biomarker and meso-tetra (4-sulfonatophenyl) porphine (TPPS4) as an optical probe, quinalphos can be selectively detected. The molecular recognition between TPPS4 and HQO leads to a considerable sensitivity of the detection. The spectral responses of TPPS4 show a linear dependence on quinalphos concentration in the presence of plant-esterase within the 0.01-1 mg kg(-1) range. The detection limit is 0.01 mg kg(-1), well below the maximum residue limits (MRLs) defined by European Union (0.05 mg kg(-1)) and China (0.2 mg kg(-1))." @default.
- W2317323979 created "2016-06-24" @default.
- W2317323979 creator A5009649294 @default.
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- W2317323979 creator A5044954885 @default.
- W2317323979 creator A5071037763 @default.
- W2317323979 creator A5078265101 @default.
- W2317323979 date "2015-05-07" @default.
- W2317323979 modified "2023-10-15" @default.
- W2317323979 title "Conversion of Inhibition Biosensing to Substrate-Like Biosensing for Quinalphos Selective Detection" @default.
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- W2317323979 doi "https://doi.org/10.1021/acs.analchem.5b00376" @default.
- W2317323979 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25921798" @default.
- W2317323979 hasPublicationYear "2015" @default.
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