Versatile method of cholinesterase immobilisation via affinity bonds using Concanavalin A applied to the construction of a screen-printed biosensor
Development of new and more reliable methods to immobilise biomolecules has emerged rapidly due to a continuous need for more stable, sensitive and reliable biosensors. This paper reports a new method of acetylcholine-esterase (AChE) immobilisation based on the high affinity interaction between the...
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| Veröffentlicht in: | Biosensors & bioelectronics 2004-09, Vol.20 (2), p.217-225 |
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| creator | Bucur, Bogdan Danet, Andrei Florin Marty, Jean-Louis |
| description | Development of new and more reliable methods to immobilise biomolecules has emerged rapidly due to a continuous need for more stable, sensitive and reliable biosensors. This paper reports a new method of acetylcholine-esterase (AChE) immobilisation based on the high affinity interaction between the glycoproteic enzyme and Concanavalin A (Con A). In order to establish the nature of the link formed between the glycoenzyme, lectin and support, three different configurations are presented. The optimum immobilisation procedure was further used for biosensor manufacturing. The non-specific adsorption is around 3% and the chemical cross-linking of the proteins is avoided. The optimised method allows loading of the working electrode surface with different amounts of enzyme ranging from 0.3 to 3.3
mIU with a good operational stability. The sensor showed a linear response range to acetylthiocholine substrate between 10 and 110
μmol
l
−1 with a sensitivity of 3.6
mA
l
mol
−1. The applicability of the method to the detection of organophosphorus insecticides resulted in a detection limit of 10
−8
mol
l
−1 for chlorpyriphos. |
| doi_str_mv | 10.1016/j.bios.2004.02.024 |
| format | Article |
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mIU with a good operational stability. The sensor showed a linear response range to acetylthiocholine substrate between 10 and 110
μmol
l
−1 with a sensitivity of 3.6
mA
l
mol
−1. The applicability of the method to the detection of organophosphorus insecticides resulted in a detection limit of 10
−8
mol
l
−1 for chlorpyriphos.</description><identifier>ISSN: 0956-5663</identifier><identifier>EISSN: 1873-4235</identifier><identifier>DOI: 10.1016/j.bios.2004.02.024</identifier><identifier>PMID: 15308225</identifier><language>eng</language><publisher>Lausanne: Elsevier B.V</publisher><subject>Acetylcholine esterase ; Affinity immobilisation ; Biological and medical sciences ; Biosensing Techniques - instrumentation ; Biosensing Techniques - methods ; Biosensors ; Biotechnology ; Cholinesterases - analysis ; Cholinesterases - chemistry ; Coated Materials, Biocompatible - chemistry ; Concanavalin A ; Concanavalin A - analysis ; Concanavalin A - chemistry ; Electrochemistry - instrumentation ; Electrochemistry - methods ; Enzyme Activation ; Enzymes, Immobilized - analysis ; Enzymes, Immobilized - chemistry ; Equipment Design ; Equipment Failure Analysis ; Fundamental and applied biological sciences. Psychology ; Methods. Procedures. Technologies ; Pesticides - analysis ; Pesticides - chemistry ; Protein Binding ; Reproducibility of Results ; Screen-printed biosensors ; Sensitivity and Specificity ; Various methods and equipments</subject><ispartof>Biosensors & bioelectronics, 2004-09, Vol.20 (2), p.217-225</ispartof><rights>2004 Elsevier B.V.</rights><rights>2005 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c413t-80b1823e313938a8222e93bfb2898865c741583d66f8792ba5660d2199851ee13</citedby><cites>FETCH-LOGICAL-c413t-80b1823e313938a8222e93bfb2898865c741583d66f8792ba5660d2199851ee13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bios.2004.02.024$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16092357$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15308225$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bucur, Bogdan</creatorcontrib><creatorcontrib>Danet, Andrei Florin</creatorcontrib><creatorcontrib>Marty, Jean-Louis</creatorcontrib><title>Versatile method of cholinesterase immobilisation via affinity bonds using Concanavalin A applied to the construction of a screen-printed biosensor</title><title>Biosensors & bioelectronics</title><addtitle>Biosens Bioelectron</addtitle><description>Development of new and more reliable methods to immobilise biomolecules has emerged rapidly due to a continuous need for more stable, sensitive and reliable biosensors. This paper reports a new method of acetylcholine-esterase (AChE) immobilisation based on the high affinity interaction between the glycoproteic enzyme and Concanavalin A (Con A). In order to establish the nature of the link formed between the glycoenzyme, lectin and support, three different configurations are presented. The optimum immobilisation procedure was further used for biosensor manufacturing. The non-specific adsorption is around 3% and the chemical cross-linking of the proteins is avoided. The optimised method allows loading of the working electrode surface with different amounts of enzyme ranging from 0.3 to 3.3
mIU with a good operational stability. The sensor showed a linear response range to acetylthiocholine substrate between 10 and 110
μmol
l
−1 with a sensitivity of 3.6
mA
l
mol
−1. The applicability of the method to the detection of organophosphorus insecticides resulted in a detection limit of 10
−8
mol
l
−1 for chlorpyriphos.</description><subject>Acetylcholine esterase</subject><subject>Affinity immobilisation</subject><subject>Biological and medical sciences</subject><subject>Biosensing Techniques - instrumentation</subject><subject>Biosensing Techniques - methods</subject><subject>Biosensors</subject><subject>Biotechnology</subject><subject>Cholinesterases - analysis</subject><subject>Cholinesterases - chemistry</subject><subject>Coated Materials, Biocompatible - chemistry</subject><subject>Concanavalin A</subject><subject>Concanavalin A - analysis</subject><subject>Concanavalin A - chemistry</subject><subject>Electrochemistry - instrumentation</subject><subject>Electrochemistry - methods</subject><subject>Enzyme Activation</subject><subject>Enzymes, Immobilized - analysis</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Equipment Design</subject><subject>Equipment Failure Analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Methods. Procedures. Technologies</subject><subject>Pesticides - analysis</subject><subject>Pesticides - chemistry</subject><subject>Protein Binding</subject><subject>Reproducibility of Results</subject><subject>Screen-printed biosensors</subject><subject>Sensitivity and Specificity</subject><subject>Various methods and equipments</subject><issn>0956-5663</issn><issn>1873-4235</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kcuKFDEUhoMoTjv6Ai4kG91Vm0ulKgE3Q-MNBtyo25BKnbLTVCVtTrphnsMXNmU3zE44kM13Tv4LIa8523LGu_eH7RASbgVj7ZaJOu0TsuG6l00rpHpKNsyorlFdJ2_IC8QDY6znhj0nN1xJpoVQG_LnJ2R0JcxAFyj7NNI0Ub9Pc4iABbJDoGFZ0hDmsHIp0nNw1E1TiKE80CHFEekJQ_xFdyl6F93Z1WV6R93xOAcYaUm07IH6FLHkk_93o37iKPoMEJtjDrFUbjUDEVN-SZ5NbkZ4dX1vyY9PH7_vvjT33z5_3d3dN77lsjSaDVwLCZJLI7WrfgQYOUyD0EbrTvm-5UrLsesm3RsxuJoEGwU3RisOwOUteXe5e8zp96natUtAD_PsIqQTWt4r3TJlKiguoM8JMcNkq-bF5QfLmV2rsAe7qrdrFZaJOm1denO9fhoWGB9XrtlX4O0VcOjdPGUXfcBHrmOm1thX7sOFg5rFOUC26ANED2PI4IsdU_ifjr_1Jqli</recordid><startdate>20040915</startdate><enddate>20040915</enddate><creator>Bucur, Bogdan</creator><creator>Danet, Andrei Florin</creator><creator>Marty, Jean-Louis</creator><general>Elsevier B.V</general><general>Elsevier Science</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20040915</creationdate><title>Versatile method of cholinesterase immobilisation via affinity bonds using Concanavalin A applied to the construction of a screen-printed biosensor</title><author>Bucur, Bogdan ; Danet, Andrei Florin ; Marty, Jean-Louis</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c413t-80b1823e313938a8222e93bfb2898865c741583d66f8792ba5660d2199851ee13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Acetylcholine esterase</topic><topic>Affinity immobilisation</topic><topic>Biological and medical sciences</topic><topic>Biosensing Techniques - instrumentation</topic><topic>Biosensing Techniques - methods</topic><topic>Biosensors</topic><topic>Biotechnology</topic><topic>Cholinesterases - analysis</topic><topic>Cholinesterases - chemistry</topic><topic>Coated Materials, Biocompatible - chemistry</topic><topic>Concanavalin A</topic><topic>Concanavalin A - analysis</topic><topic>Concanavalin A - chemistry</topic><topic>Electrochemistry - instrumentation</topic><topic>Electrochemistry - methods</topic><topic>Enzyme Activation</topic><topic>Enzymes, Immobilized - analysis</topic><topic>Enzymes, Immobilized - chemistry</topic><topic>Equipment Design</topic><topic>Equipment Failure Analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Methods. Procedures. Technologies</topic><topic>Pesticides - analysis</topic><topic>Pesticides - chemistry</topic><topic>Protein Binding</topic><topic>Reproducibility of Results</topic><topic>Screen-printed biosensors</topic><topic>Sensitivity and Specificity</topic><topic>Various methods and equipments</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bucur, Bogdan</creatorcontrib><creatorcontrib>Danet, Andrei Florin</creatorcontrib><creatorcontrib>Marty, Jean-Louis</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Biosensors & bioelectronics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bucur, Bogdan</au><au>Danet, Andrei Florin</au><au>Marty, Jean-Louis</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Versatile method of cholinesterase immobilisation via affinity bonds using Concanavalin A applied to the construction of a screen-printed biosensor</atitle><jtitle>Biosensors & bioelectronics</jtitle><addtitle>Biosens Bioelectron</addtitle><date>2004-09-15</date><risdate>2004</risdate><volume>20</volume><issue>2</issue><spage>217</spage><epage>225</epage><pages>217-225</pages><issn>0956-5663</issn><eissn>1873-4235</eissn><abstract>Development of new and more reliable methods to immobilise biomolecules has emerged rapidly due to a continuous need for more stable, sensitive and reliable biosensors. This paper reports a new method of acetylcholine-esterase (AChE) immobilisation based on the high affinity interaction between the glycoproteic enzyme and Concanavalin A (Con A). In order to establish the nature of the link formed between the glycoenzyme, lectin and support, three different configurations are presented. The optimum immobilisation procedure was further used for biosensor manufacturing. The non-specific adsorption is around 3% and the chemical cross-linking of the proteins is avoided. The optimised method allows loading of the working electrode surface with different amounts of enzyme ranging from 0.3 to 3.3
mIU with a good operational stability. The sensor showed a linear response range to acetylthiocholine substrate between 10 and 110
μmol
l
−1 with a sensitivity of 3.6
mA
l
mol
−1. The applicability of the method to the detection of organophosphorus insecticides resulted in a detection limit of 10
−8
mol
l
−1 for chlorpyriphos.</abstract><cop>Lausanne</cop><pub>Elsevier B.V</pub><pmid>15308225</pmid><doi>10.1016/j.bios.2004.02.024</doi><tpages>9</tpages></addata></record> |
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| subjects | Acetylcholine esterase Affinity immobilisation Biological and medical sciences Biosensing Techniques - instrumentation Biosensing Techniques - methods Biosensors Biotechnology Cholinesterases - analysis Cholinesterases - chemistry Coated Materials, Biocompatible - chemistry Concanavalin A Concanavalin A - analysis Concanavalin A - chemistry Electrochemistry - instrumentation Electrochemistry - methods Enzyme Activation Enzymes, Immobilized - analysis Enzymes, Immobilized - chemistry Equipment Design Equipment Failure Analysis Fundamental and applied biological sciences. Psychology Methods. Procedures. Technologies Pesticides - analysis Pesticides - chemistry Protein Binding Reproducibility of Results Screen-printed biosensors Sensitivity and Specificity Various methods and equipments |
| title | Versatile method of cholinesterase immobilisation via affinity bonds using Concanavalin A applied to the construction of a screen-printed biosensor |
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