ReversE · Modifying Enzyme with Solid-Binding Peptide for Site-specific and Reversible Enzyme Immobilization
„Хоризонт Европа“ — Действия „Мария Склодовска-Кюри“
- Период
- 2023-08-01 → 2025-07-31
- Финансиране от ЕС
- 189 687 €
- Участници
- 1
- Схема
- HORIZON-TMA-MSCA-PF-EF
Линиите свързват координатора с партньорите.
Накратко на български
Ензимите, които ускоряват процеси като производството на водород, се модифицират, за да се закрепят и отделят контролирано от повърхността на електроди. Това помага за обновяването на системите и удължава работата им при преобразуване на енергия.
Кратко обяснение, генерирано от езиков модел по текста на CORDIS. Оригиналът е по-долу.
Резултати накратко
Modifying Enzyme with Solid-Binding Peptide for Site-specific and Reversible Enzyme Immobilization
ReversE (Modifying enzyme with solid-binding peptide for site-specific and reversible enzyme immobilization) aims to address a key question, with a special focus on the longevity of the labile enzyme-based systems, which remains a bottleneck in enzyme-electrode biotechnological applications. Redox enzymes catalyze numerous biological processes, such as hydrogen evolution and uptake, carbon dioxide reduction, and nitrogen reduction, which are also relevant for a variety of applications, including enzymatic biofuel cells and the electrosynthesis of complex molecules. However, enzyme’s limited stability diminishes their potential to be exploited in biotechnological applications. The project’s overall goal is to develop a reversible immobilization approach that can attach enzymes on an electrode surface in a defined orientation and enable its controlled release on demand upon stimulation. This paves the way for enzyme regeneration on the electrode surface, which will be groundbreaking in the context of sustainable deployment of enzyme‒electrode systems. To accomplish this goal, the project is structured around three core objectives. Objective 1 – To genetically engineer redox metalloenzymes for site-specific immobilization Objective 2 – To establish methods for releasing bound enzymes from electrodes under mild conditions, preserving the properties of the electrode surface, and allowing new cycles of enzyme immobilization Objective 3 – To demonstrate the practical use of the reversible binding for device reusability and prolonged operation in energy-conversion applications Pathway to impact Scientific: the findings are crucial for fundamental understanding of intricate mechanisms behind the association and dissociation of solid-binding peptide-fused enzyme on the solid electrode surface. Technological: develop a blueprint for a reusable enzyme-electrode suitable for practical implementation in future technologies. Industrial & economic: enables the regeneration of devices, making future enzymatic biofuel cells and biosensor technologies more sustainable, which would otherwise be hampered by costly and elaborate surface modifications. Societal & environmental: the reuse of gold or other solid electrodes supports the objectives of the European Green Deal by minimizing environmental impact and decreasing reliance on critical raw materials.
Текст от CORDIS, на английски · Данни: CORDIS, © Европейски съюз
Цел на проекта
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.
Оригинален текст от CORDIS (на английски).
Участници
- TECHNISCHE UNIVERSITAET MUENCHEN · MuenchenКоординаторГермания
Връзки
- Виж в CORDIS
- DOI: 10.3030/101110795
- https://ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e508354a89&appId=PPGMS
- https://ec.europa.eu/research/participants/documents/downloadPublic?documentIds=080166e522a00171&appId=PPGMS
Данни: CORDIS, © Европейски съюз
