Journal
SENSORS AND ACTUATORS B-CHEMICAL
Volume 148, Issue 1, Pages 17-22Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.snb.2010.04.023
Keywords
Copper, zinc superoxide dismutase; Horseradish peroxidase; Cysteine biosensor; Polypyrrole
Funding
- Department of Biotechnology, New Delhi, India [BT/PR6153/MED/14/748/2005]
- Managing Board of Virudhunagar Hindu Nadars' Senthikumara Nadar College, Virudhunagar, Tamil Nadu, India
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A new cysteine (CySH) biosensor was developed based on its oxidase-peroxidase activities with copper, zinc superoxide dismutase (SOD1). The biosensor comprising of SOD1 coimmobilized with horseradish peroxidase (HRP) on polypyrrole (PPy)-platinum (Pt) electrode was characterized by cyclic voltammetry. The bienzymatic electrode exhibited an electrochemical response with cysteine due to the bicarbonate-dependent peroxidase activity stimulated by thiol oxidase activity of SOD1. Among the thiols, viz, CySH, HCY and GSH. CySH only showed a remarkable amplification of current. Thus, the biosensor is CySH selective. The electrode linearly responded to cysteine concentrations up to 500 mu M with a detection limit of 10 mu M. The CySH biosensor is highly stable, selective and reproducible, making it suitable for analytical purposes. Using this biosensor, the levels of CySH present in commercially available L-CySH dietary supplement tablets, serum and urine were estimated. (C) 2010 Elsevier B.V. All rights reserved.
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