Laser Interference Pattern Ablation of a Carbon Fiber Microelectrode: Biosensor Signal Enhancement after Enzyme Attachment
Fluorescence microscopy was used to visualize the accumulated fluorescent product of the enzyme alkaline phosphatase to indicate where active covalently bound enzyme remained on the surface after application of a Nd:YAG laser interference pattern to a surface that was first globally derivatized with...
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| Veröffentlicht in: | Analytical chemistry (Washington) 2000-10, Vol.72 (20), p.4914-4920 |
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| creator | Rosenwald, Steven E Nowall, Wilbur B Dontha, Narasaiah Kuhr, Werner G |
| description | Fluorescence microscopy was used to visualize the accumulated fluorescent product of the enzyme alkaline phosphatase to indicate where active covalently bound enzyme remained on the surface after application of a Nd:YAG laser interference pattern to a surface that was first globally derivatized with the covalently bound enzyme. The electrochemical kinetics of the same carbon fiber surface were examined through the electrogenerated chemiluminescence of Ru(bpy)3 2+ to determine that electron-transfer sites were indeed segregated from the enzyme-binding sites. The enzyme-derivatized areas are determined to be separate and distinct from the areas of enhanced electron transfer. Two other enzymes, glucose oxidase and malic dehydrogenase, were then covalently bound to carbon fiber microelectrode surfaces in order to verify the change in detection limit of their respective cofactors, NADH or H2O2, under a variety of surface conditions. The S/N of an enzyme-modified electrode after laser interference pattern photoablation and electrocatalytic treatment is improved by more than 1 order of magnitude over that observed at an electrode that is globally enzyme modified. |
| doi_str_mv | 10.1021/ac000442t |
| format | Article |
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The electrochemical kinetics of the same carbon fiber surface were examined through the electrogenerated chemiluminescence of Ru(bpy)3 2+ to determine that electron-transfer sites were indeed segregated from the enzyme-binding sites. The enzyme-derivatized areas are determined to be separate and distinct from the areas of enhanced electron transfer. Two other enzymes, glucose oxidase and malic dehydrogenase, were then covalently bound to carbon fiber microelectrode surfaces in order to verify the change in detection limit of their respective cofactors, NADH or H2O2, under a variety of surface conditions. 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| subjects | Biological and medical sciences Biosensing Techniques Biosensors Biotechnology Carbon - chemistry Chemical bonds Enzymes Fluorescence Fundamental and applied biological sciences. Psychology Glucose Oxidase - chemistry Lasers Malate Dehydrogenase - chemistry Methods. Procedures. Technologies Microelectrodes Various methods and equipments |
| title | Laser Interference Pattern Ablation of a Carbon Fiber Microelectrode: Biosensor Signal Enhancement after Enzyme Attachment |
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