Electrical activity of cellobiose dehydrogenase adsorbed on thiols: Influence of charge and hydrophobicity
| Autor: | Miguel D. Toscano, Peter Lamberg, Sergey Shleev, J. Hamit-Eminovski, Gediminas Niaura, Tautgirdas Ruzgas, O. Eicher-Lorka, Thomas Arnebrant |
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| Rok vydání: | 2017 |
| Předmět: |
Cellobiose dehydrogenase
Biophysics 02 engineering and technology 010402 general chemistry Photochemistry Electrochemistry 01 natural sciences Catalysis chemistry.chemical_compound Electron transfer Ascomycota Monolayer Organic chemistry Sulfhydryl Compounds Surface charge Physical and Theoretical Chemistry Self-assembled monolayer General Medicine Quartz crystal microbalance Enzymes Immobilized 021001 nanoscience & nanotechnology Elasticity 0104 chemical sciences chemistry Quartz Crystal Microbalance Techniques Carbohydrate Dehydrogenases Adsorption Gold Pyridinium 0210 nano-technology Hydrophobic and Hydrophilic Interactions |
| Zdroj: | Bioelectrochemistry. 115:26-32 |
| ISSN: | 1567-5394 |
| DOI: | 10.1016/j.bioelechem.2017.02.001 |
| Popis: | The interface between protein and material surface is of great research interest in applications varying from implants, tissue engineering to bioelectronics. Maintaining functionality of bioelements depends greatly on the immobilization process. In the present study direct electron transfer of cellobiose dehydrogenase from Humicola insolens ( Hi CDH), adsorbed on four different self-assembled monolayers (SAMs) formed by 5–6 chain length carbon thiols varying in terminal group structure was investigated. By using a combination of quartz crystal microbalance with dissipation, ellipsometry and electrochemistry the formation and function of the Hi CDH film was studied. It was found that the presence of charged pyridinium groups was needed to successfully establish direct electron contact between the enzyme and electrode. SAMs formed from hydrophilic charged thiols achieved nearly two times higher current densities compared to hydrophobic charged thiols. Additionally, the results also indicated proportionality between Hi CDH catalytic constant and water content of the enzyme film. Enzyme films on charged pyridine thiols had smaller variations in water content and viscoelastic properties than films adsorbed on the more hydrophobic thiols. This work highlights several perspectives on the underlying factors affecting performance of immobilized Hi CDH. |
| Databáze: | OpenAIRE |
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