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| Main Authors: | , , , , , , , |
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| Format: | Preprint |
| Published: |
2025
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| Subjects: | |
| Online Access: | https://arxiv.org/abs/2503.14308 |
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| _version_ | 1866917959994179584 |
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| author | Serial, M. Raquel Schmidt, Luca Adrian, Muhammad Brauckmann, Grit Benders, Stefan Bueschler, Victoria Liese, Andreas Penn, Alexander |
| author_facet | Serial, M. Raquel Schmidt, Luca Adrian, Muhammad Brauckmann, Grit Benders, Stefan Bueschler, Victoria Liese, Andreas Penn, Alexander |
| contents | Enzyme immobilization plays a crucial role in enhancing the stability and recyclability of enzymes for industrial applications. However, traditional methods for quantifying enzyme loading within porous carriers are limited by time-consuming workflows, cumulative errors, and the inability to probe enzymes adsorbed inside the pores. In this study, we introduce Time-Domain Nuclear Magnetic Resonance (TD-NMR) relaxometry as a novel, non-invasive technique for directly quantifying enzyme adsorption within porous carriers. Focusing on epoxy methyl acrylate carriers, commonly used in biocatalysis, we correlate changes in T2 relaxation times with enzyme concentration, leading to the development of an NMR-based pore-filling ratio that quantifies enzyme loading. Validation experiments demonstrate that TD-NMR-derived adsorption curves align closely with traditional photometric measurements, offering a reliable and reproducible alternative for enzyme quantification. The accessibility of tabletop TD-NMR spectrometers makes this technique a practical and cost-effective tool for optimizing biocatalytic processes. Furthermore, the method holds promise for real-time monitoring of adsorption dynamics and could be adapted for a wider range of carrier materials and enzymes. |
| format | Preprint |
| id |
arxiv_https___arxiv_org_abs_2503_14308 |
| institution | arXiv |
| publishDate | 2025 |
| record_format | arxiv |
| spellingShingle | A novel method for quantifying enzyme immobilization in porous carriers using simple NMR relaxometry Serial, M. Raquel Schmidt, Luca Adrian, Muhammad Brauckmann, Grit Benders, Stefan Bueschler, Victoria Liese, Andreas Penn, Alexander Soft Condensed Matter Enzyme immobilization plays a crucial role in enhancing the stability and recyclability of enzymes for industrial applications. However, traditional methods for quantifying enzyme loading within porous carriers are limited by time-consuming workflows, cumulative errors, and the inability to probe enzymes adsorbed inside the pores. In this study, we introduce Time-Domain Nuclear Magnetic Resonance (TD-NMR) relaxometry as a novel, non-invasive technique for directly quantifying enzyme adsorption within porous carriers. Focusing on epoxy methyl acrylate carriers, commonly used in biocatalysis, we correlate changes in T2 relaxation times with enzyme concentration, leading to the development of an NMR-based pore-filling ratio that quantifies enzyme loading. Validation experiments demonstrate that TD-NMR-derived adsorption curves align closely with traditional photometric measurements, offering a reliable and reproducible alternative for enzyme quantification. The accessibility of tabletop TD-NMR spectrometers makes this technique a practical and cost-effective tool for optimizing biocatalytic processes. Furthermore, the method holds promise for real-time monitoring of adsorption dynamics and could be adapted for a wider range of carrier materials and enzymes. |
| title | A novel method for quantifying enzyme immobilization in porous carriers using simple NMR relaxometry |
| topic | Soft Condensed Matter |
| url | https://arxiv.org/abs/2503.14308 |