Activity of glucose oxidase functionalized onto magnetic nanoparticles

Gilles K Kouassi¹ , Joseph Irudayaraj¹ and Gregory McCarty²

¹Department of Agricultural and Biological Engineering, The Pennsylvania State University, University Park, PA 16802, USA

²Department of Engineering Sciences and Mechanics, The Pennsylvania State University, University Park, PA 16802, USA

author email corresponding author email

BioMagnetic Research and Technology 2005, 3:1doi:10.1186/1477-044X-3-1


Published:	11 March 2005

Abstract

Background

Magnetic nanoparticles have been significantly used for coupling with biomolecules, due to their unique properties.

Methods

Magnetic nanoparticles were synthesized by thermal co-precipitation of ferric and ferrous chloride using two different base solutions. Glucose oxidase was bound to the particles by direct attachment via carbodiimide activation or by thiophene acetylation of magnetic nanoparticles. Transmission electron microscopy was used to characterize the size and structure of the particles while the binding of glucose oxidase to the particles was confirmed using Fourier transform infrared spectroscopy.

Results

The direct binding of glucose oxidase via carbodiimide activity was found to be more effective, resulting in bound enzyme efficiencies between 94–100% while thiophene acetylation was 66–72% efficient. Kinetic and stability studies showed that the enzyme activity was more preserved upon binding onto the nanoparticles when subjected to thermal and various pH conditions. The overall activity of glucose oxidase was improved when bound to magnetic nanoparticles

Conclusion

Binding of enzyme onto magnetic nanoparticles via carbodiimide activation is a very efficient method for developing bioconjugates for biological applications