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A novel method for quantifying enzyme immobilization in porous carriers using simple NMR relaxometry
Citation Link: https://doi.org/10.15480/882.15901
Publikationstyp
Journal Article
Date Issued
2025-08-29
Sprache
English
Author(s)
Serial, M. Raquel
TORE-DOI
Journal
Volume
225
Article Number
109909
Citation
Biochemical Engineering Journal 225: 109909 (2026)
Publisher DOI
Scopus ID
Publisher
Elsevier
Peer Reviewed
true
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 T<inf>2</inf> 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.
Subjects
Adsorption isotherms
Enzyme immobilization
Pore-filling ratio
Porous carriers
TD-NMR relaxometry
DDC Class
572: Biochemistry
660: Chemistry; Chemical Engineering
Publication version
publishedVersion
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