Development of an enzyme-based biosensor for atrazine detection

Fiona A. McArdle; Krishna C. Persaud

doi:10.1039/AN9931800419

Development of an enzyme-based biosensor for atrazine detection

Fiona A. McArdle, Krishna C. Persaud

Research output: Contribution to journal › Article › peer-review

Abstract

An amperometric biosensor for detection of the photosynthetic inhibiting herbicide atrazine is described. The sensor, incorporating the enzyme tyrosinase, was sensitive to a wide range of di- and triphenols. It displayed a fast response, with 95% of the steady-state current being obtained within 25 s, and had a half-life of 8 d but retained some activity for up to 20 d. This biosensor displayed a notable decrease in response in the presence of atrazine. Atrazine inhibition of the biosensor response was found to be reversible. The electrode construction consisted of tyrosinase cross-linked on a poly(pyrrole) coated gold electrode surface. The inhibition of enzyme activity in the presence of atrazine was measured amperometrically. Atrazine concentrations of 5 × 10-6 mol dm-3 were measured in a hydrodynamic cell and of 1 × 10-5 mol dm-3 in a flow-through system.

Original language	English
Pages (from-to)	419-423
Number of pages	4
Journal	Analyst
Volume	4
Issue number	118
DOIs	https://doi.org/10.1039/AN9931800419
Publication status	Published - 1993

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title = "Development of an enzyme-based biosensor for atrazine detection",

abstract = "An amperometric biosensor for detection of the photosynthetic inhibiting herbicide atrazine is described. The sensor, incorporating the enzyme tyrosinase, was sensitive to a wide range of di- and triphenols. It displayed a fast response, with 95% of the steady-state current being obtained within 25 s, and had a half-life of 8 d but retained some activity for up to 20 d. This biosensor displayed a notable decrease in response in the presence of atrazine. Atrazine inhibition of the biosensor response was found to be reversible. The electrode construction consisted of tyrosinase cross-linked on a poly(pyrrole) coated gold electrode surface. The inhibition of enzyme activity in the presence of atrazine was measured amperometrically. Atrazine concentrations of 5 × 10-6 mol dm-3 were measured in a hydrodynamic cell and of 1 × 10-5 mol dm-3 in a flow-through system.",

author = "McArdle, {Fiona A.} and Persaud, {Krishna C.}",

note = "Times Cited: 54 SYMP ON SENSORS AND SIGNALS, AT THE 1992 AUTUMN MEETING OF THE ROYAL SOC OF CHEMISTRY SEP 16-18, 1992 TRINITY COLL, DUBLIN, IRELAND",

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doi = "10.1039/AN9931800419",

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T1 - Development of an enzyme-based biosensor for atrazine detection

AU - McArdle, Fiona A.

AU - Persaud, Krishna C.

N1 - Times Cited: 54 SYMP ON SENSORS AND SIGNALS, AT THE 1992 AUTUMN MEETING OF THE ROYAL SOC OF CHEMISTRY SEP 16-18, 1992 TRINITY COLL, DUBLIN, IRELAND

PY - 1993

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N2 - An amperometric biosensor for detection of the photosynthetic inhibiting herbicide atrazine is described. The sensor, incorporating the enzyme tyrosinase, was sensitive to a wide range of di- and triphenols. It displayed a fast response, with 95% of the steady-state current being obtained within 25 s, and had a half-life of 8 d but retained some activity for up to 20 d. This biosensor displayed a notable decrease in response in the presence of atrazine. Atrazine inhibition of the biosensor response was found to be reversible. The electrode construction consisted of tyrosinase cross-linked on a poly(pyrrole) coated gold electrode surface. The inhibition of enzyme activity in the presence of atrazine was measured amperometrically. Atrazine concentrations of 5 × 10-6 mol dm-3 were measured in a hydrodynamic cell and of 1 × 10-5 mol dm-3 in a flow-through system.

AB - An amperometric biosensor for detection of the photosynthetic inhibiting herbicide atrazine is described. The sensor, incorporating the enzyme tyrosinase, was sensitive to a wide range of di- and triphenols. It displayed a fast response, with 95% of the steady-state current being obtained within 25 s, and had a half-life of 8 d but retained some activity for up to 20 d. This biosensor displayed a notable decrease in response in the presence of atrazine. Atrazine inhibition of the biosensor response was found to be reversible. The electrode construction consisted of tyrosinase cross-linked on a poly(pyrrole) coated gold electrode surface. The inhibition of enzyme activity in the presence of atrazine was measured amperometrically. Atrazine concentrations of 5 × 10-6 mol dm-3 were measured in a hydrodynamic cell and of 1 × 10-5 mol dm-3 in a flow-through system.

U2 - 10.1039/AN9931800419

DO - 10.1039/AN9931800419

M3 - Article

SN - 0003-2654

VL - 4

SP - 419

EP - 423

JO - Analyst

JF - Analyst

IS - 118

ER -

Development of an enzyme-based biosensor for atrazine detection

Abstract

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