Biosensor based on cellobiose dehydrogenase for detection of catecholamines.
Identifieur interne : 000899 ( Main/Exploration ); précédent : 000898; suivant : 000900Biosensor based on cellobiose dehydrogenase for detection of catecholamines.
Auteurs : Leonard Stoica [Suède] ; Annika Lindgren-Sjölander ; Tautgirdas Ruzgas ; Lo GortonSource :
- Analytical chemistry [ 0003-2700 ] ; 2004.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , analysis : Catecholamines.
- chemical , metabolism : Carbohydrate Dehydrogenases.
- Biosensing Techniques, Flavin-Adenine Dinucleotide, Indicators and Reagents, Sensitivity and Specificity.
Abstract
A cellobiose dehydrogenase (CDH)-modified graphite electrode was designed for amperometric detection of catecholamines in the flow injection mode, by their recycling between the graphite electrode (+300 mV vs Ag|AgCl) and the reduced FAD cofactor of adsorbed CDH, resulting in an amplified response signal. The high efficiency of the enzyme-catecholamine reaction leads to a detection limit below 1 nM and a sensitivity of 15.8 A.M(-1) x cm(-2) (approximately 1150 nA/microM) for noradrenaline, with a coverage of less than 2.5 microg of CDH adsorbed on the electrode surface (0.073 cm(2)). Working parameters such as pH, cellobiose concentration, carrier buffer, and applied potential were optimized, using hydroquinone as a model analyte. The sensitivity, linear range, and amplification factor can be modulated by the steady-state concentration of cellobiose in the flow buffer. The response of the sensor decreases only 2% when run continuously for 4 h in the flow injection mode. The response peak maximum is obtained within 6 s at a flow rate of 0.5 mL/min, representing the time of the entire sample segment to pass the electrode. CDH enzymes from Phanerochaete chrysosporium and Sclerotium rolfsii were investigated, providing different characteristics of the sensor, with sensors made with CDH from P. chrysosporium being the better ones.
DOI: 10.1021/ac049582j
PubMed: 15307778
Affiliations:
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Box 124, SE-22100 Lund</wicri:regionArea><wicri:noRegion>SE-22100 Lund</wicri:noRegion></affiliation></author><author><name sortKey="Lindgren Sjolander, Annika" sort="Lindgren Sjolander, Annika" uniqKey="Lindgren Sjolander A" first="Annika" last="Lindgren-Sjölander">Annika Lindgren-Sjölander</name></author><author><name sortKey="Ruzgas, Tautgirdas" sort="Ruzgas, Tautgirdas" uniqKey="Ruzgas T" first="Tautgirdas" last="Ruzgas">Tautgirdas Ruzgas</name></author><author><name sortKey="Gorton, Lo" sort="Gorton, Lo" uniqKey="Gorton L" first="Lo" last="Gorton">Lo Gorton</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2004">2004</date><idno type="RBID">pubmed:15307778</idno><idno type="pmid">15307778</idno><idno type="doi">10.1021/ac049582j</idno><idno type="wicri:Area/Main/Corpus">000886</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000886</idno><idno type="wicri:Area/Main/Curation">000886</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000886</idno><idno type="wicri:Area/Main/Exploration">000886</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Biosensor based on cellobiose dehydrogenase for detection of catecholamines.</title><author><name sortKey="Stoica, Leonard" sort="Stoica, Leonard" uniqKey="Stoica L" first="Leonard" last="Stoica">Leonard Stoica</name><affiliation wicri:level="1"><nlm:affiliation>Department of Analytical Chemistry, Lund University, P.O. Box 124, SE-22100 Lund, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Analytical Chemistry, Lund University, P.O. Box 124, SE-22100 Lund</wicri:regionArea><wicri:noRegion>SE-22100 Lund</wicri:noRegion></affiliation></author><author><name sortKey="Lindgren Sjolander, Annika" sort="Lindgren Sjolander, Annika" uniqKey="Lindgren Sjolander A" first="Annika" last="Lindgren-Sjölander">Annika Lindgren-Sjölander</name></author><author><name sortKey="Ruzgas, Tautgirdas" sort="Ruzgas, Tautgirdas" uniqKey="Ruzgas T" first="Tautgirdas" last="Ruzgas">Tautgirdas Ruzgas</name></author><author><name sortKey="Gorton, Lo" sort="Gorton, Lo" uniqKey="Gorton L" first="Lo" last="Gorton">Lo Gorton</name></author></analytic><series><title level="j">Analytical chemistry</title><idno type="ISSN">0003-2700</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biosensing Techniques (MeSH)</term><term>Carbohydrate Dehydrogenases (metabolism)</term><term>Catecholamines (analysis)</term><term>Flavin-Adenine Dinucleotide (MeSH)</term><term>Indicators and Reagents (MeSH)</term><term>Sensitivity and Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Carbohydrate dehydrogenases (métabolisme)</term><term>Catécholamines (analyse)</term><term>Flavine adénine dinucléotide (MeSH)</term><term>Indicateurs et réactifs (MeSH)</term><term>Sensibilité et spécificité (MeSH)</term><term>Techniques de biocapteur (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Catecholamines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carbohydrate Dehydrogenases</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Catécholamines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Carbohydrate dehydrogenases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biosensing Techniques</term><term>Flavin-Adenine Dinucleotide</term><term>Indicators and Reagents</term><term>Sensitivity and Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Flavine adénine dinucléotide</term><term>Indicateurs et réactifs</term><term>Sensibilité et spécificité</term><term>Techniques de biocapteur</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A cellobiose dehydrogenase (CDH)-modified graphite electrode was designed for amperometric detection of catecholamines in the flow injection mode, by their recycling between the graphite electrode (+300 mV vs Ag|AgCl) and the reduced FAD cofactor of adsorbed CDH, resulting in an amplified response signal. The high efficiency of the enzyme-catecholamine reaction leads to a detection limit below 1 nM and a sensitivity of 15.8 A.M(-1) x cm(-2) (approximately 1150 nA/microM) for noradrenaline, with a coverage of less than 2.5 microg of CDH adsorbed on the electrode surface (0.073 cm(2)). Working parameters such as pH, cellobiose concentration, carrier buffer, and applied potential were optimized, using hydroquinone as a model analyte. The sensitivity, linear range, and amplification factor can be modulated by the steady-state concentration of cellobiose in the flow buffer. The response of the sensor decreases only 2% when run continuously for 4 h in the flow injection mode. The response peak maximum is obtained within 6 s at a flow rate of 0.5 mL/min, representing the time of the entire sample segment to pass the electrode. CDH enzymes from Phanerochaete chrysosporium and Sclerotium rolfsii were investigated, providing different characteristics of the sensor, with sensors made with CDH from P. chrysosporium being the better ones.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15307778</PMID><DateCompleted><Year>2006</Year><Month>05</Month><Day>02</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-2700</ISSN><JournalIssue CitedMedium="Print"><Volume>76</Volume><Issue>16</Issue><PubDate><Year>2004</Year><Month>Aug</Month><Day>15</Day></PubDate></JournalIssue><Title>Analytical chemistry</Title><ISOAbbreviation>Anal Chem</ISOAbbreviation></Journal><ArticleTitle>Biosensor based on cellobiose dehydrogenase for detection of catecholamines.</ArticleTitle><Pagination><MedlinePgn>4690-6</MedlinePgn></Pagination><Abstract><AbstractText>A cellobiose dehydrogenase (CDH)-modified graphite electrode was designed for amperometric detection of catecholamines in the flow injection mode, by their recycling between the graphite electrode (+300 mV vs Ag|AgCl) and the reduced FAD cofactor of adsorbed CDH, resulting in an amplified response signal. The high efficiency of the enzyme-catecholamine reaction leads to a detection limit below 1 nM and a sensitivity of 15.8 A.M(-1) x cm(-2) (approximately 1150 nA/microM) for noradrenaline, with a coverage of less than 2.5 microg of CDH adsorbed on the electrode surface (0.073 cm(2)). Working parameters such as pH, cellobiose concentration, carrier buffer, and applied potential were optimized, using hydroquinone as a model analyte. The sensitivity, linear range, and amplification factor can be modulated by the steady-state concentration of cellobiose in the flow buffer. The response of the sensor decreases only 2% when run continuously for 4 h in the flow injection mode. The response peak maximum is obtained within 6 s at a flow rate of 0.5 mL/min, representing the time of the entire sample segment to pass the electrode. CDH enzymes from Phanerochaete chrysosporium and Sclerotium rolfsii were investigated, providing different characteristics of the sensor, with sensors made with CDH from P. chrysosporium being the better ones.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Stoica</LastName><ForeName>Leonard</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Analytical Chemistry, Lund University, P.O. Box 124, SE-22100 Lund, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lindgren-Sjölander</LastName><ForeName>Annika</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Ruzgas</LastName><ForeName>Tautgirdas</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Gorton</LastName><ForeName>Lo</ForeName><Initials>L</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Anal Chem</MedlineTA><NlmUniqueID>0370536</NlmUniqueID><ISSNLinking>0003-2700</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002395">Catecholamines</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007202">Indicators and Reagents</NameOfSubstance></Chemical><Chemical><RegistryNumber>146-14-5</RegistryNumber><NameOfSubstance UI="D005182">Flavin-Adenine Dinucleotide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D002237">Carbohydrate Dehydrogenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.99.18</RegistryNumber><NameOfSubstance UI="C019859">cellobiose-quinone oxidoreductase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D015374" MajorTopicYN="Y">Biosensing Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002237" MajorTopicYN="N">Carbohydrate Dehydrogenases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002395" MajorTopicYN="N">Catecholamines</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005182" MajorTopicYN="N">Flavin-Adenine Dinucleotide</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007202" MajorTopicYN="N">Indicators and Reagents</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012680" MajorTopicYN="N">Sensitivity and Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>8</Month><Day>17</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>5</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>8</Month><Day>17</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15307778</ArticleId><ArticleId IdType="doi">10.1021/ac049582j</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country></list><tree><noCountry><name sortKey="Gorton, Lo" sort="Gorton, Lo" uniqKey="Gorton L" first="Lo" last="Gorton">Lo Gorton</name><name sortKey="Lindgren Sjolander, Annika" sort="Lindgren Sjolander, Annika" uniqKey="Lindgren Sjolander A" first="Annika" last="Lindgren-Sjölander">Annika Lindgren-Sjölander</name><name sortKey="Ruzgas, Tautgirdas" sort="Ruzgas, Tautgirdas" uniqKey="Ruzgas T" first="Tautgirdas" last="Ruzgas">Tautgirdas Ruzgas</name></noCountry><country name="Suède"><noRegion><name sortKey="Stoica, Leonard" sort="Stoica, Leonard" uniqKey="Stoica L" first="Leonard" last="Stoica">Leonard Stoica</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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