Literature DB >> 19132842

Interaction of D-amino acid oxidase with carbon nanotubes: implications in the design of biosensors.

Maria F Mora1, Carla E Giacomelli, Carlos D Garcia.   

Abstract

We have investigated the interaction of d-amino acid oxidase (DAAO) with single-walled carbon nanotubes (CNT) by spectroscopic ellipsometry. Dynamic adsorption experiments were performed at different experimental conditions. In addition, the activity of the enzyme adsorbed at different conditions was studied. Our results indicate that DAAO can be adsorbed to CNT at different pH values and concentrations by a combination of hydrophobic and electrostatic interactions. Considering that the highest enzymatic activity was obtained by adsorbing the protein at pH 5.7 and 0.1 mg x mL(-1), our results indicate that DAAO can adopt multiple orientations on the surface, which are ultimately responsible for significant differences in catalytic activity.

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Year:  2009        PMID: 19132842      PMCID: PMC2646172          DOI: 10.1021/ac802068n

Source DB:  PubMed          Journal:  Anal Chem        ISSN: 0003-2700            Impact factor:   6.986


  52 in total

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8.  Carbon nanotube-chitosan system for electrochemical sensing based on dehydrogenase enzymes.

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Review 9.  Carbon nanotubes for electrochemical biosensing.

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10.  Determination of D-amino acid oxidase activity in tumour cells.

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  19 in total

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4.  Adsorption of Glucose Oxidase to 3-D Scaffolds of Carbon Nanotubes: Analytical Applications.

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Journal:  Electroanalysis       Date:  2011-05-12       Impact factor: 3.223

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7.  Determination of a setup correction function to obtain adsorption kinetic data at stagnation point flow conditions.

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Review 8.  Protein adsorption onto nanomaterials for the development of biosensors and analytical devices: a review.

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9.  Ultrathin optically transparent carbon electrodes produced from layers of adsorbed proteins.

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10.  Spectroscopic and electrochemical characterization of nanostructured optically transparent carbon electrodes.

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Journal:  Electrophoresis       Date:  2013-06-21       Impact factor: 3.535

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