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  <doc>
    <id>580</id>
    <completedYear>2011</completedYear>
    <publishedYear/>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst/>
    <pageLast/>
    <pageNumber>10</pageNumber>
    <edition/>
    <issue>46</issue>
    <volume>9</volume>
    <type>article</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>1</belongsToBibliography>
    <completedDate>2016-06-16</completedDate>
    <publishedDate>2011-10-07</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Light triggered detection of aminophenyl phosphate with a quantum dot based enzyme electrode</title>
    <abstract language="eng">An electrochemical sensor for p-aminophenyl phosphate (p APP) is reported. It is based on the electrochemical conversion of 4-aminophenol (4AP) at a quantum dot (QD) modified electrode under illumination. Without illumination no electron transfer and thus no oxidation of 4AP can occur. p APP as substrate is converted by the enzyme alkaline phosphatase (ALP) to generate 4AP as a product. The QDs are coupled via 1,4-benzenedithiol (BDT) linkage to the surface of a gold electrode and thus allow potential-controlled photocurrent generation. The photocurrent is modified by the enzyme reaction providing access to the substrate detection. In order to develop a photobioelectrochemical sensor the enzyme is immobilized on top of the photo-switchable layer of the QDs. Immobilization of ALP is required for the potential possibility of spatially resolved measurements. Geometries with immobilized ALP are compared versus having the ALP in solution. Data indicate that functional immobilization with layer-by-layer assembly is possible. Enzymatic activity of ALP and thus the photocurrent can be described by Michaelis- Menten kinetics. p APP is detected as proof of principle investigation within the range of 25 μM - 1 mM.</abstract>
    <parentTitle language="eng">Journal of Nanobiotechnology</parentTitle>
    <identifier type="issn">1477-3155</identifier>
    <identifier type="urn">urn:nbn:de:kobv:526-opus4-5808</identifier>
    <enrichment key="SourceTitle">Khalid, W., Göbel, G., Hühn, D. et al. Light triggered detection of aminophenyl phosphate with a quantum dot based enzyme electrode. J Nanobiotechnol 9, 46 (2011). https://doi.org/10.1186/1477-3155-9-46</enrichment>
    <enrichment key="DOI_VoR">https://doi.org/10.1186/1477-3155-9-46</enrichment>
    <licence>Creative Commons - CC BY - Namensnennung 2.0 Generic</licence>
    <author>Waqas Khalid</author>
    <author>Gero Göbel</author>
    <author>Dominik Hühn</author>
    <author>Jose-Maria Montenegro</author>
    <author>Pilar Rivera-Gil</author>
    <author>Fred Lisdat</author>
    <author>Wolfgang J. Parak</author>
    <collection role="ddc" number="660">Chemische Verfahrenstechnik</collection>
    <collection role="institutes" number="">Fachbereich Ingenieurwesen / Wirtschaftsingenieurwesen (bis 8/2014)</collection>
    <collection role="open_access" number="">open_access</collection>
    <collection role="green_open_access" number="1">Gold Open Access</collection>
    <thesisPublisher>Technische Hochschule Wildau</thesisPublisher>
    <file>https://opus4.kobv.de/opus4-th-wildau/files/580/2F1477-3155-9-46.pdf</file>
  </doc>
  <doc>
    <id>81</id>
    <completedYear>2011</completedYear>
    <publishedYear>2011</publishedYear>
    <thesisYearAccepted/>
    <language>deu</language>
    <pageFirst>13</pageFirst>
    <pageLast>21</pageLast>
    <pageNumber/>
    <edition/>
    <issue/>
    <volume>15</volume>
    <type>articlewildau</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>1</belongsToBibliography>
    <completedDate>--</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="deu">Entwicklung einer Glucosedehydrogenase-basierten Anode und deren Anwendung in einer Glucose/O2-Biobrennstoffzelle</title>
    <abstract language="deu">Unter Verwendung von mehrwandigen Kohlenstoffnanoröhren wurde in dieser Studie eine neuartige Anode zum Einsatz in Biobrennstoffzellen entwickelt. Dazu wurde das rekombinante Enzym Pyrrolochinolinchinon(PQQ)- abhängige Glucosedehydrogenase kovalent an eine aus PQQ bestehenden Zwischenschicht gekoppelt, welche zuvor an die Kohlenstoffnanoröhren adsorbiert war. Die Nanoröhren wurden aufgrund ihrer Thiolmodifikation chemisorptiv auf einer Goldelektrode gebunden. In glucosehaltiger Lösung konnte der Start eines katalytischen Stroms bei einem Potential von -80 mV vs. Ag/AgCl (1 MKCl) beobachtet werden. Unter Substratsättigung wurden Stromdichten im Bereich von 170 bis 200 μA/cm2 gemessen. Dieses System basiert auf einem mediatorvermittelten Elektronentransfer. Die entwickelte (PQQ)-GDH-MWCNT-Elektrode wurde mit einer MWCNT-modifizierten Elektrode kombiniert, bei der Bilirubinoxidase (BOD) als Biokatalysator fungiert. Daraus resultierte eine membranfreie Biobrennstoffzelle mit einem leichgewichtspotential von 600 mV und Leistungsdichten im Bereich von 20-25 μW/cm2.</abstract>
    <abstract language="eng">In this study a biofuel cell anode is developed on the basis of multi-walled carbon nanotubes (MWCNTs). Recombinant pyrroloquinoline quinone (PQQ) dependent glucose dehydrogenase is covalently coupled to a PQQ-layer which is adsorbed onto thiolmodified MWCNTs. The MWCNTs are chemisorbed to a gold electrode. In the presence of glucose a catalytic current starts at a potential of -80 mV vs. Ag/AgCl, 1 M KCl. Under substrate saturation current densities of 170 to 200 μA/cm2 can be achieved. The operation is based on mediated electron transfer of the enzyme. This (PQQ)-GDH-MWCNT-electrode is combined with a MWCNT-modifi ed electrode to which bilirubin oxidase (BOD) is covalently coupled. The resulting membrane-free biofuel cell has an open cell potential of 600 mV and can achieve power densities in the range of 20-25 μW/cm2.</abstract>
    <parentTitle language="deu">Wissenschaftliche Beiträge 2011</parentTitle>
    <identifier type="issn">0949-8214</identifier>
    <identifier type="urn">urn:nbn:de:kobv:526-opus-1039</identifier>
    <identifier type="opus3-id">103</identifier>
    <identifier type="doi">10.15771/0949-8214_2011_1_2</identifier>
    <enrichment key="InvalidVerification">123</enrichment>
    <enrichment key="ZSTiteliD">16238</enrichment>
    <licence>Creative Commons - CC BY-NC-ND 3.0 DE - Namensnennung - Nicht-kommerziell - Keine Bearbeitung 3.0 Deutschland</licence>
    <author>Christoph K. Tanne</author>
    <author>Gero Göbel</author>
    <author>Fred Lisdat</author>
    <collection role="ddc" number="572">Biochemie</collection>
    <collection role="ddc" number="621">Angewandte Physik</collection>
    <collection role="institutes" number="">Fachbereich Ingenieurwesen / Wirtschaftsingenieurwesen (bis 8/2014)</collection>
    <collection role="Publikationen_der_TH_Wildau" number="">Wissenschaftliche Beiträge</collection>
    <collection role="open_access" number="">open_access</collection>
    <thesisPublisher>Technische Hochschule Wildau</thesisPublisher>
    <file>https://opus4.kobv.de/opus4-th-wildau/files/81/TH_WB2011_Beitrag02_Tanne_Goebel_Lisdat.pdf</file>
  </doc>
</export-example>
