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ReversE

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

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

31/07/2025

TUM

190K€

Presupuesto del proyecto: 190K€

Líder del proyecto

TECHNISCHE UNIVERSITAET MUENCHEN No se ha especificado una descripción o un objeto social para esta compañía.

TRL 4-5

Financiación concedida El organismo HORIZON EUROPE notifico la concesión del proyecto el día 2023-03-21

HORIZON-MSCA-2022-PF-01-01: MSCA Postdoctoral Fellowships 2022 ExpectedOutcome:

I+D

Cerrada hace 2 años

0% 100% 100%

1 Participantes

TUM

189.69K€ | Lider

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Duración del proyecto: 28 meses Fecha Inicio: 2023-03-21
Fecha Fin: 2025-07-31

Líder del proyecto

TECHNISCHE UNIVERSITAET MUENCHEN No se ha especificado una descripción o un objeto social para esta compañía.

TRL 4-5

Presupuesto del proyecto 190K€

Descripción del proyecto 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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