Preparing Catalytic Surfaces for Sensing Applications by Immobilizing Enzymes via Hydrophobin Layers
- 17 February 2005
- journal article
- research article
- Published by American Chemical Society (ACS) in Analytical Chemistry
- Vol. 77 (6) , 1622-1630
- https://doi.org/10.1021/ac048897w
Abstract
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 Schizophyllumcommune 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.Keywords
This publication has 41 references indexed in Scilit:
- Structural changes and molecular interactions of hydrophobin SC3 in solution and on a hydrophobic surfaceProtein Science, 2002
- Coming up for air and sporulationNature, 1999
- Glucose Oxidase as an Analytical ReagentCritical Reviews in Analytical Chemistry, 1995
- Crystal Structure of Glucose Oxidase from Aspergillus niger Refined at 2·3 Å ReslutionJournal of Molecular Biology, 1993
- Effects of carbohydrate depletion on the structure, stability and activity of glucose oxidase from Aspergillus nigerBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
- Structural model of vinculin: Correlation of amino acid sequence with electron‐microscopical shapeFEBS Letters, 1989
- Biosensors: fundamentals and applicationsAnalytica Chimica Acta, 1987
- Interactive computer animation of macromoleculesJournal of Molecular Graphics, 1984
- Covalent structure of the glycoprotein horseradish peroxidase (EC 1.11.1.7)FEBS Letters, 1976
- A role of the carbohydrate moiety of glucose oxidase: Kinetic evidence for protection of the enzyme from thermal inactivation in the presence of sodium dodecyl sulfateFEBS Letters, 1974