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Modifying Enzyme with Solid-Binding Peptide for Site-specific and Reversible Enzyme Immobilization

Project description

Towards improved enzyme-electrode systems

Reduction-oxidation (redox) enzymes facilitate chemical reactions involving the transfer of electrons between molecules. These enzymes are essential in various biological processes, including cellular respiration, photosynthesis, and the metabolism of various compounds. They have also been explored in applications that involve energy conversion, biosensing, and electrosynthesis. However, their limited stability and the challenge of aligning them with electrode surfaces hinder their widespread use. Funded by the Marie Skłodowska-Curie Actions programme, the ReversE project aims to develop a reversible immobilisation method to attach enzymes to electrodes with precise orientation. This approach will enable the controlled release of enzymes upon stimulation, allowing for their regeneration and sustainable deployment in enzyme-electrode systems.

Objective

Redox enzymes catalyze numerous biological processes that are also relevant for a variety of applications, including energy conversion, biosensing, and electrosynthesis of complex molecules. The intrinsic lability of enzymes that gradually lose catalytic activity over time, however, restricts their operational half-life for practical large-scale application of this sustainable and incredibly energy-saving system. Moreover, enzymes are nanometer-sized macromolecules, that must be properly aligned with the electrode surface for efficient electron transfer and substrate access to the active site regardless of the electron transfer mechanism, direct or mediated, which typically necessitates laborious procedures. The goal of this Marie Skłodowska-Curie Postdoctoral Fellowship project is to develop a reversible immobilization approach that can attach enzymes on an electrode surface in a defined orientation and permit their controlled release on demand upon stimulation (ReversE). This will be accomplished by capitalizing on a gold (Au)-binding peptide fused to [FeFe]-hydrogenase as the model enzyme to have the dual functionality of orienting enzymes on the Au electrode surface in a precise manner to support efficient electron transfer and substrate access to the active site, as well as allowing the bound Au-binding peptide fused enzymes to be released by electrochemical or chemical stimuli and replaced with fresh enzymes when the catalytic activity is reduced to a predetermined value. This will open up the possibility for enzyme regeneration which will be groundbreaking in the context of sustainable deployment of enzyme‒electrode systems.

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HORIZON-TMA-MSCA-PF-EF - HORIZON TMA MSCA Postdoctoral Fellowships - European Fellowships

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Call for proposal

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(opens in new window) HORIZON-MSCA-2022-PF-01

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Coordinator

TECHNISCHE UNIVERSITAET MUENCHEN
Net EU contribution

Net EU financial contribution. The sum of money that the participant receives, deducted by the EU contribution to its linked third party. It considers the distribution of the EU financial contribution between direct beneficiaries of the project and other types of participants, like third-party participants.

€ 189 687,36
Address
Arcisstrasse 21
80333 Muenchen
Germany

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Region
Bayern Oberbayern München, Kreisfreie Stadt
Activity type
Higher or Secondary Education Establishments
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Total cost

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