Preparing catalytic surfaces for sensing applications by immobilizing enzymes via hydrophobin layers.
Simple and reliable immobilization techniques that preserve the activity of enzymes are of interest in many technologies based on catalysis. Here, two redox enzymes, glucose oxidase from Aspergillus niger and horseradish peroxidase, were immobilized by physisorption on glassy carbon electrodes coated with Schizophyllum commune hydrophobin. Hydrophobins are small, interfacially active proteins that have the remarkable property of adhering to almost any surface. We showed recently that these proteins can be used to immobilize small, electroactive molecules. The results obtained in this work show a way to easily manufacture stable, enzyme-based catalytic surfaces for applications in biosensing.
Corvis
Yohann
Y
Groupe d'Etude des Vecteurs Supramoléculaires du Médicament UMR 7565 CNRS/Université Henri Poincaré Nancy 1, Faculté des Sciences, BP 239, 54506 Vandoeuvre-lès-Nancy Cedex, France.
Walcarius
Alain
A
Rink
Rick
R
Mrabet
Nadir T
NT
Rogalska
Ewa
E
D015374:Biosensing Techniques / Q000379:methods*; D002384:Catalysis; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry*; D005949:Glucose Oxidase / Q000737:chemistry; D006735:Horseradish Peroxidase / Q000737:chemistry; D013499:Surface Properties
D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D005949:Glucose Oxidase; D006735:Horseradish Peroxidase