Title of article :
Receptor binding protein amperometric affinity sensor for rapid β-lactam quantification in milk Original Research Article
Author/Authors :
S.J. Setford، نويسنده , , R.M. Van Es، نويسنده , , Y.J. Blankwater، نويسنده , , S. Kr?ger، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 1999
Pages :
10
From page :
13
To page :
22
Abstract :
Screen-printed devices, incorporating working electrode immobilised β-lactam specific receptor binding protein, were employed to measure penicillin G levels in milk. Quantification was achieved through ELISA-based affinity-assay format coupled to amperometric determination of bound enzyme label activity. Assay inhibition increased from zero, in the absence of penicillin G in milk, to 33.5 and 77.1% reduction in signal response in the presence of 5 μg kg−1 and 10 μg kg−1 penicillin G, respectively. The maximum residue limit of penicillin G in milk for consumption is 5 μg kg−1, as defined by the FDA. Coefficient of variation values varied from 4.2–26.4%. The assay incorporates a 2–4 min incubation step, a rapid washing step and 1–2 min measurement step. The receptor binding protein is specific for the major β-lactam antibiotic types. The assay is simple to perform and requires minimum reagent usage, making it ideal as a field-based screening tool for β-lactam quantification in milk.
Keywords :
Milk , Screen-printed electrodes , Receptor binding protein , ?-lactam , Amperometry , Affinity sensor , Antibiotic , Penicillin G
Journal title :
Analytica Chimica Acta
Serial Year :
1999
Journal title :
Analytica Chimica Acta
Record number :
1027967
Link To Document :
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