| 47458 |
Creator |
3d9f5a6838060f791e133fa6e5265b06 |
| 47458 |
Creator |
ext-732a277ea47bfb5d46643ed37419f5e1 |
| 47458 |
Creator |
ext-9c82bad4b92590ab5aa9934ebed1a25a |
| 47458 |
Creator |
ext-a1ead9211e2394d2777624e645f1f7d0 |
| 47458 |
Creator |
ext-a64ca8a2630c00fddeb98600fb9762cb |
| 47458 |
Creator |
ext-ce6761ea7288b9c44fdd363cbbbae284 |
| 47458 |
Date |
2016-09-23 |
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Is Part Of |
repository |
| 47458 |
Is Part Of |
pb9d57d86d1f23d8098e2d4ebfa5e4117 |
| 47458 |
abstract |
Al doped and undoped ZnO thin films were deposited by pulsed-laser deposition on polycarbonate
sheets. The films were characterized by optical transmission, Hall effect measurement,
XRD and SEM. Optical transmission and surface reflectometry studies showed good transparency
with thicknesses ∼100 nm and surface roughness of 10 nm. Hall effect measurements
showed that the sheet carrier concentration was −1.44 × 10<sup>15</sup> cm<sup>−2</sup>
for AZO and −6 × 10<sup>14</sup> cm<sup>−2</sup> for ZnO. The films were then modified
by drop-casting glucose oxidase (GOx) without the use of any mediators. Higher protein
concentration was observed on ZnO as compared to AZO with higher specific activity
for ZnO (0.042 U mg<sup>−1</sup>) compared to AZO (0.032 U mg<sup>−1</sup>), and was
in agreement with cyclic voltemmetry (CV). X-ray photoelectron spectroscopy (XPS)
suggested that the protein was bound by dipole interactions between AZO lattice oxygen
and the amino group of the enzyme. Chronoamperometry showed sensitivity of 5.5 μA
mM<sup>−1</sup> cm<sup>−2</sup> towards glucose for GOx/AZO and 2.2 μA mM<sup>−1</sup>
cm<sup>−2</sup> for GOx/ZnO. The limit of detection (LoD) was 167 μM of glucose for
GOx/AZO, as compared to 360 μM for GOx/ZnO. The linearity was 0.28–28 mM for GOx/AZO
whereas it was 0.6–28 mM for GOx/ZnO with a response time of 10s. Possibly due to
higher enzyme loading, the decrease of impedance in presence of glucose was larger
for GOx/ZnO as compared to GOx/AZO in electrochemical impedance spectroscopy (EIS).
Analyses with clinical blood serum samples showed that the systems had good reproducibility
and accuracy. The characteristics of novel ZnO and AZO thin films with GOx as a model
enzyme, should prove useful for the future fabrication of inexpensive, highly sensitive,
disposable electrochemical biosensors for high throughput diagnostics. |
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authorList |
authors |
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status |
peerReviewed |
| 47458 |
uri |
http://data.open.ac.uk/oro/document/513427 |
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uri |
http://data.open.ac.uk/oro/document/513429 |
| 47458 |
uri |
http://data.open.ac.uk/oro/document/513430 |
| 47458 |
uri |
http://data.open.ac.uk/oro/document/513431 |
| 47458 |
uri |
http://data.open.ac.uk/oro/document/513432 |
| 47458 |
uri |
http://data.open.ac.uk/oro/document/513433 |
| 47458 |
uri |
http://data.open.ac.uk/oro/document/513578 |
| 47458 |
type |
AcademicArticle |
| 47458 |
type |
Article |
| 47458 |
label |
Kumar, Fidal; Inguva, Saikumar; Krishnamurthy, Satheesh ; Marsili, Enrico; Mosnier,
Jean-Paul and Sainathan, Chandra (2016). Mediator-free interaction of glucose oxidase,
as model enzyme for immobilization, with Al-doped and undoped ZnO thin films laser-deposited
on polycarbonate supports. Enzyme and Microbial Technology (In Press). |
| 47458 |
label |
Kumar, Fidal; Inguva, Saikumar; Krishnamurthy, Satheesh ; Marsili, Enrico; Mosnier,
Jean-Paul and Sainathan, Chandra (2016). Mediator-free interaction of glucose oxidase,
as model enzyme for immobilization, with Al-doped and undoped ZnO thin films laser-deposited
on polycarbonate supports. Enzyme and Microbial Technology (In Press). |
| 47458 |
Title |
Mediator-free interaction of glucose oxidase, as model enzyme for immobilization,
with Al-doped and undoped ZnO thin films laser-deposited on polycarbonate supports |
| 47458 |
in dataset |
oro |