Counting the number of enzymes immobilized onto a nanoparticle-coated electrode
Journal article, 2018

To immobilize enzymes at the surface of a nanoparticle-based electrochemical sensor is a common method to construct biosensors for non-electroactive analytes. Studying the interactions between the enzymes and nanoparticle support is of great importance in optimizing the conditions for biosensor design. This can be achieved by using a combination of analytical methods to carefully characterize the enzyme nanoparticle coating at the sensor surface while studying the optimal conditions for enzyme immobilization. From this analytical approach, it was found that controlling the enzyme coverage to a monolayer was a key factor to significantly improve the temporal resolution of biosensors. However, these characterization methods involve both tedious methodologies and working with toxic cyanide solutions. Here we introduce a new analytical method that allows direct quantification of the number of immobilized enzymes (glucose oxidase) at the surface of a gold nanoparticle coated glassy carbon electrode. This was achieved by exploiting an electrochemical stripping method for the direct quantification of the density and size of gold nanoparticles coating the electrode surface and combining this information with quantification of fluorophore-labeled enzymes bound to the sensor surface after stripping off their nanoparticle support. This method is both significantly much faster compared to previously reported methods and with the advantage that this method presented is non-toxic.

Electrochemical stripping

Microelectrode

Enzyme quantification

Glucose oxidase

Immobilized enzyme

Gold nanoparticles

Author

Jenny Bergman

University of Gothenburg

Yuanmo Wang

Chalmers, Chemistry and Chemical Engineering, Chemistry and Biochemistry, Analytical Chemistry

Joakim Wigström

Chalmers, Chemistry and Chemical Engineering, Chemistry and Biochemistry, Analytical Chemistry

Ann-Sofie Cans

Chalmers, Chemistry and Chemical Engineering, Chemistry and Biochemistry

Analytical and Bioanalytical Chemistry

1618-2642 (ISSN) 1618-2650 (eISSN)

Vol. 410 6 1775-1783

Subject Categories

Analytical Chemistry

Materials Chemistry

Other Chemistry Topics

DOI

10.1007/s00216-017-0829-1

PubMed

29279991

More information

Latest update

5/8/2018 6