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A selective nitric oxide nanocomposite biosensor based on direct electron transfer of microperoxidase: Removal of interferences by co-immobilized enzymes.

09:02 EDT 18th May 2013 | BioPortfolio

Summary of "A selective nitric oxide nanocomposite biosensor based on direct electron transfer of microperoxidase: Removal of interferences by co-immobilized enzymes."

A highly selective nitric oxide (NO) biosensor was developed by immobilizing microperoxidase (MP) onto the MWCNT-poly-5,2':5',2″-terthiophene-3'-carboxylic acid (PTTCA) nanocomposite. Catalase (CAS) and superoxide dismutase (SOD) co-immobilized on the probe successfully protected the interferences of H(2)O(2) and O(2)(-) during NO detection. The nanocomposite layer showed the direct electron transfer processes of the immobilized CAS, SOD, and MP simultaneously at -0.11/+0.04, -0.33/-0.27, and -0.47/-0.40V vs. Ag/AgCl. Au nanoparticles (AuNPs) were electrodeposited on a glassy carbon surface to enhance the sensitivity of the sensor probe. The layers of CAS/SOD/MP/MWCNT-PTTCA/AuNPs were characterized using SEM, XPS, and QCM. The CAS/SOD/MP/MWCNT-PTTCA/AuNPs probe showed an excellent performance in the electrocatalytic reduction of NO which was attributed to the heme group of MP. Experimental conditions affecting the sensitivity of the biosensor were optimized in terms of pH, temperature, and applied potential. The dynamic range of NO analysis was from 1.0 to 40μM with the detection limit of 4.3±0.2nM. The reliability of biosensor was examined for the determination of NO released from the real samples of rat liver, stomach (AGS), and intestinal (HT-29) cancer cells.

Affiliation

Department of Chemistry and Institute of BioPhysio Sensor Technology, Pusan National University, Busan 609-735, South Korea.

Journal Details

This article was published in the following journal.

Name: Biosensors & bioelectronics
ISSN: 1873-4235
Pages:

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Medical and Biotech [MESH] Definitions

Nitric Oxide

A free radical gas produced endogenously by a variety of mammalian cells, synthesized from ARGININE by NITRIC OXIDE SYNTHASE. Nitric oxide is one of the ENDOTHELIUM-DEPENDENT RELAXING FACTORS released by the vascular endothelium and mediates VASODILATION. It also inhibits platelet aggregation, induces disaggregation of aggregated platelets, and inhibits platelet adhesion to the vascular endothelium. Nitric oxide activates cytosolic GUANYLATE CYCLASE and thus elevates intracellular levels of CYCLIC GMP.

Nitric Oxide Synthase

An NADPH-dependent enzyme that catalyzes the conversion of L-ARGININE and OXYGEN to produce CITRULLINE and NITRIC OXIDE.

Nitric Oxide Synthase Type I

A CALCIUM-dependent, constitutively-expressed form of nitric oxide synthase found primarily in NERVE TISSUE.

Nitric Oxide Synthase Type Iii

A CALCIUM-dependent, constitutively-expressed form of nitric oxide synthase found primarily in ENDOTHELIAL CELLS.

Nitric Oxide Synthase Type Ii

A CALCIUM-independent subtype of nitric oxide synthase that may play a role in immune function. It is an inducible enzyme whose expression is transcriptionally regulated by a variety of CYTOKINES.

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