This work presents an inhibition-based biosensor for the fast, simple and inexpensive determination of atrazine. The method is based on the inhibition of the enzyme tyrosinase from mushrooms (Tyr), immobilized on screen printed electrodes (SPEs). To optimize the biosensor performances several carbon based SPEs: graphite (G), graphene (GP), and multiwalled carbon nanotubes (MWCNTs) and immobilization techniques (physical and chemical) have been tested. Tyrosinase was immobilized on the electrode surface by either polyvinyl alcohol with styrylpyridinium groups (PVA-SbQ) as cross-linking agent or Nafion membranes as physical entrapment or bovine serum albumin with glutaraldehyde as chemical immobilization. In the presence of catechol as substrate, atrazine can be determined thanks to its inhibition activity towards the enzyme which catalyzes the oxidation of catechol to o-quinone. Under optimum experimental conditions, the best performance in terms of catalytic efficiency has been demonstrated by MWCNTs screen printed electrode with PVA-SbQ as immobilization method. The developed inhibition biosensor displays a linearity range towards atrazine within 0.5–20 ppm, a LOD of 0.3 ppm and acceptable repeatability and stability. This analysis method was applied to spiked drinking water samples with recoveries close to 95% respect to measurements carried out in PBS buffer. The low cost of this device and its good analytical performances suggest its application for the screening and monitoring of atrazine in real matrices.

Inhibition-based biosensor for atrazine detection / Tortolini, Cristina; Bollella, Paolo; Antiochia, Riccarda; Favero, Gabriele; Mazzei, Franco. - In: SENSORS AND ACTUATORS. B, CHEMICAL. - ISSN 0925-4005. - STAMPA. - 224:(2016), pp. 552-558. [10.1016/j.snb.2015.10.095]

Inhibition-based biosensor for atrazine detection

TORTOLINI, CRISTINA;BOLLELLA, PAOLO;ANTIOCHIA, RICCARDA;FAVERO, Gabriele;MAZZEI, Franco
2016

Abstract

This work presents an inhibition-based biosensor for the fast, simple and inexpensive determination of atrazine. The method is based on the inhibition of the enzyme tyrosinase from mushrooms (Tyr), immobilized on screen printed electrodes (SPEs). To optimize the biosensor performances several carbon based SPEs: graphite (G), graphene (GP), and multiwalled carbon nanotubes (MWCNTs) and immobilization techniques (physical and chemical) have been tested. Tyrosinase was immobilized on the electrode surface by either polyvinyl alcohol with styrylpyridinium groups (PVA-SbQ) as cross-linking agent or Nafion membranes as physical entrapment or bovine serum albumin with glutaraldehyde as chemical immobilization. In the presence of catechol as substrate, atrazine can be determined thanks to its inhibition activity towards the enzyme which catalyzes the oxidation of catechol to o-quinone. Under optimum experimental conditions, the best performance in terms of catalytic efficiency has been demonstrated by MWCNTs screen printed electrode with PVA-SbQ as immobilization method. The developed inhibition biosensor displays a linearity range towards atrazine within 0.5–20 ppm, a LOD of 0.3 ppm and acceptable repeatability and stability. This analysis method was applied to spiked drinking water samples with recoveries close to 95% respect to measurements carried out in PBS buffer. The low cost of this device and its good analytical performances suggest its application for the screening and monitoring of atrazine in real matrices.
2016
atrazine; inhibition biosensor; screen printed electrode; tyrosinase; electrical and electronic engineering; condensed matter physics; electronic, optical and magnetic materials; 2506; surfaces, coatings and films; materials chemistry2506 metals and alloys; instrumentation
01 Pubblicazione su rivista::01a Articolo in rivista
Inhibition-based biosensor for atrazine detection / Tortolini, Cristina; Bollella, Paolo; Antiochia, Riccarda; Favero, Gabriele; Mazzei, Franco. - In: SENSORS AND ACTUATORS. B, CHEMICAL. - ISSN 0925-4005. - STAMPA. - 224:(2016), pp. 552-558. [10.1016/j.snb.2015.10.095]
File allegati a questo prodotto
File Dimensione Formato  
Tortolini_Inhibition-based_2016.pdf

solo gestori archivio

Tipologia: Versione editoriale (versione pubblicata con il layout dell'editore)
Licenza: Tutti i diritti riservati (All rights reserved)
Dimensione 703.95 kB
Formato Adobe PDF
703.95 kB Adobe PDF   Contatta l'autore

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/839232
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 54
  • ???jsp.display-item.citation.isi??? 49
social impact