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Tyrosinase Biosensor for Antioxidants Based on Semiconducting Polymer Support
This study reports sensitive phenolic compounds detection using biosensing electrode constructed by immobilization of tyrosinase in an electrochemically synthesized copolymer based on N‐nonylcarbazole derivatives on a platinum (Pt) electrode. Tyrosinase has been successfully immobilized (electrolyti...
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Published in: | Electroanalysis (New York, N.Y.) N.Y.), 2016-06, Vol.28 (6), p.1383-1390 |
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creator | Cabaj, Joanna Jędrychowska, Agnieszka Świst, Agnieszka Sołoducho, Jadwiga |
description | This study reports sensitive phenolic compounds detection using biosensing electrode constructed by immobilization of tyrosinase in an electrochemically synthesized copolymer based on N‐nonylcarbazole derivatives on a platinum (Pt) electrode. Tyrosinase has been successfully immobilized (electrolytic deposition) on the surface of thin film built of poly[2,7‐bis(selenophene)‐N‐nonylcarbazole] and poly[3,6‐bis(selenophene)‐N‐nonylcarbazole]. A well‐defined reduction current according to the phenolic compounds was observed in cyclic voltammetry, which assigned to the reduction of biocatalytically produced o‐quinones on the electrode surface. The immersion of the tyrosinase‐equipped electrode in solution with substrate generated large catalytic currents easily recorded by cyclic voltammetry. The response of the biosensing arrangement was estimated in the presence of catechol and L‐3,4‐dihydroxyphenylalanine (L‐DOPA). The system exhibits an explicit catalytic activity and the substrates can be amperometrically determined at +0.07 V vs. Ag/AgCl. The activation energy (Ea) of immobilized tyrosinase catalytic reaction was estimated as 24.65 kJ/mol in PBS buffer. The analytical properties of the developed biosensor, such as linear concentration range, sensitivity, detection limit and reproducibility, repeatibility were also evaluated. Considering the fact, that the immobilization policy proved high efficiency, the results suggest that the method for phenoloxidase immobilization has a big capacity of providing high throughput engineering of bioelectronic devices. |
doi_str_mv | 10.1002/elan.201500523 |
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Tyrosinase has been successfully immobilized (electrolytic deposition) on the surface of thin film built of poly[2,7‐bis(selenophene)‐N‐nonylcarbazole] and poly[3,6‐bis(selenophene)‐N‐nonylcarbazole]. A well‐defined reduction current according to the phenolic compounds was observed in cyclic voltammetry, which assigned to the reduction of biocatalytically produced o‐quinones on the electrode surface. The immersion of the tyrosinase‐equipped electrode in solution with substrate generated large catalytic currents easily recorded by cyclic voltammetry. The response of the biosensing arrangement was estimated in the presence of catechol and L‐3,4‐dihydroxyphenylalanine (L‐DOPA). The system exhibits an explicit catalytic activity and the substrates can be amperometrically determined at +0.07 V vs. Ag/AgCl. The activation energy (Ea) of immobilized tyrosinase catalytic reaction was estimated as 24.65 kJ/mol in PBS buffer. The analytical properties of the developed biosensor, such as linear concentration range, sensitivity, detection limit and reproducibility, repeatibility were also evaluated. Considering the fact, that the immobilization policy proved high efficiency, the results suggest that the method for phenoloxidase immobilization has a big capacity of providing high throughput engineering of bioelectronic devices.</description><identifier>ISSN: 1040-0397</identifier><identifier>EISSN: 1521-4109</identifier><identifier>DOI: 10.1002/elan.201500523</identifier><language>eng</language><publisher>Weinheim: WILEY-VCH Verlag</publisher><subject>Agaricus bisporus ; Biosensors ; Catalysts ; catechol ; conducting polymer ; Electrodes ; enzymatic electrode ; Immobilization ; phenolic compounds determination ; Phenols ; Reduction (electrolytic) ; Tyrosinase ; Voltammetry</subject><ispartof>Electroanalysis (New York, N.Y.), 2016-06, Vol.28 (6), p.1383-1390</ispartof><rights>2016 WILEY‐VCH Verlag GmbH & Co. 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Tyrosinase has been successfully immobilized (electrolytic deposition) on the surface of thin film built of poly[2,7‐bis(selenophene)‐N‐nonylcarbazole] and poly[3,6‐bis(selenophene)‐N‐nonylcarbazole]. A well‐defined reduction current according to the phenolic compounds was observed in cyclic voltammetry, which assigned to the reduction of biocatalytically produced o‐quinones on the electrode surface. The immersion of the tyrosinase‐equipped electrode in solution with substrate generated large catalytic currents easily recorded by cyclic voltammetry. The response of the biosensing arrangement was estimated in the presence of catechol and L‐3,4‐dihydroxyphenylalanine (L‐DOPA). The system exhibits an explicit catalytic activity and the substrates can be amperometrically determined at +0.07 V vs. Ag/AgCl. The activation energy (Ea) of immobilized tyrosinase catalytic reaction was estimated as 24.65 kJ/mol in PBS buffer. The analytical properties of the developed biosensor, such as linear concentration range, sensitivity, detection limit and reproducibility, repeatibility were also evaluated. Considering the fact, that the immobilization policy proved high efficiency, the results suggest that the method for phenoloxidase immobilization has a big capacity of providing high throughput engineering of bioelectronic devices.</description><subject>Agaricus bisporus</subject><subject>Biosensors</subject><subject>Catalysts</subject><subject>catechol</subject><subject>conducting polymer</subject><subject>Electrodes</subject><subject>enzymatic electrode</subject><subject>Immobilization</subject><subject>phenolic compounds determination</subject><subject>Phenols</subject><subject>Reduction (electrolytic)</subject><subject>Tyrosinase</subject><subject>Voltammetry</subject><issn>1040-0397</issn><issn>1521-4109</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><recordid>eNqFkMFPgzAUh4nRxDm9eubohfnaUqDHbZmbBqfJ5ky8NFCKqQLFFuL472XBLN48NK_J-30v732Oc41gggDwrSySaoIBUQCKyYkzQhQjz0fATvs_-OABYeG5c2HtBwCwwGcj53HbGW1VlVjpzpS2srLauHn_plWj9F5lSdVYd9b3M1dX7kaWSugqa0Wjqnf3WRddKY27aetam-bSOcuTwsqr3zp2Xu4W2_nKi5-W9_Np7AkSAPEinPq5xCyDnADqt01C4VPMUgx-SlhEgzxHLJeMCohkRiIWhpDSFGUiYIJFZOzcDHNro79aaRteKitk0RuQurUcRZj6LKTA-uhkiIr-TmtkzmujysR0HAE_eOMHb_zorQfYAHyrQnb_pPkinq7_st7AKtvI_ZFNzCcPQhJS_rpe8ni1W-4eCOVv5AdspIEG</recordid><startdate>201606</startdate><enddate>201606</enddate><creator>Cabaj, Joanna</creator><creator>Jędrychowska, Agnieszka</creator><creator>Świst, Agnieszka</creator><creator>Sołoducho, Jadwiga</creator><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><scope>BSCLL</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7U5</scope><scope>8FD</scope><scope>L7M</scope></search><sort><creationdate>201606</creationdate><title>Tyrosinase Biosensor for Antioxidants Based on Semiconducting Polymer Support</title><author>Cabaj, Joanna ; Jędrychowska, Agnieszka ; Świst, Agnieszka ; Sołoducho, Jadwiga</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3603-82b4fe29d0f301052a7c4529b204b39856ff19fe95c08ed389770b5b1dc69c983</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Agaricus bisporus</topic><topic>Biosensors</topic><topic>Catalysts</topic><topic>catechol</topic><topic>conducting polymer</topic><topic>Electrodes</topic><topic>enzymatic electrode</topic><topic>Immobilization</topic><topic>phenolic compounds determination</topic><topic>Phenols</topic><topic>Reduction (electrolytic)</topic><topic>Tyrosinase</topic><topic>Voltammetry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cabaj, Joanna</creatorcontrib><creatorcontrib>Jędrychowska, Agnieszka</creatorcontrib><creatorcontrib>Świst, Agnieszka</creatorcontrib><creatorcontrib>Sołoducho, Jadwiga</creatorcontrib><collection>Istex</collection><collection>CrossRef</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Electroanalysis (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cabaj, Joanna</au><au>Jędrychowska, Agnieszka</au><au>Świst, Agnieszka</au><au>Sołoducho, Jadwiga</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tyrosinase Biosensor for Antioxidants Based on Semiconducting Polymer Support</atitle><jtitle>Electroanalysis (New York, N.Y.)</jtitle><addtitle>Electroanalysis</addtitle><date>2016-06</date><risdate>2016</risdate><volume>28</volume><issue>6</issue><spage>1383</spage><epage>1390</epage><pages>1383-1390</pages><issn>1040-0397</issn><eissn>1521-4109</eissn><abstract>This study reports sensitive phenolic compounds detection using biosensing electrode constructed by immobilization of tyrosinase in an electrochemically synthesized copolymer based on N‐nonylcarbazole derivatives on a platinum (Pt) electrode. Tyrosinase has been successfully immobilized (electrolytic deposition) on the surface of thin film built of poly[2,7‐bis(selenophene)‐N‐nonylcarbazole] and poly[3,6‐bis(selenophene)‐N‐nonylcarbazole]. A well‐defined reduction current according to the phenolic compounds was observed in cyclic voltammetry, which assigned to the reduction of biocatalytically produced o‐quinones on the electrode surface. The immersion of the tyrosinase‐equipped electrode in solution with substrate generated large catalytic currents easily recorded by cyclic voltammetry. The response of the biosensing arrangement was estimated in the presence of catechol and L‐3,4‐dihydroxyphenylalanine (L‐DOPA). The system exhibits an explicit catalytic activity and the substrates can be amperometrically determined at +0.07 V vs. Ag/AgCl. The activation energy (Ea) of immobilized tyrosinase catalytic reaction was estimated as 24.65 kJ/mol in PBS buffer. The analytical properties of the developed biosensor, such as linear concentration range, sensitivity, detection limit and reproducibility, repeatibility were also evaluated. Considering the fact, that the immobilization policy proved high efficiency, the results suggest that the method for phenoloxidase immobilization has a big capacity of providing high throughput engineering of bioelectronic devices.</abstract><cop>Weinheim</cop><pub>WILEY-VCH Verlag</pub><doi>10.1002/elan.201500523</doi><tpages>8</tpages></addata></record> |
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subjects | Agaricus bisporus Biosensors Catalysts catechol conducting polymer Electrodes enzymatic electrode Immobilization phenolic compounds determination Phenols Reduction (electrolytic) Tyrosinase Voltammetry |
title | Tyrosinase Biosensor for Antioxidants Based on Semiconducting Polymer Support |
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