10.09.2025

New publication available online!

Figure: T2 relaxation time distributions for ECR8204M carrier at three different enzyme adsorption concentrations, showing populations A, B and C

A novel method for quantifying enzyme immobilization in porous carriers by NMR relaxometry was developed by R. Serial, M. Adrian, S. Benders and A. Penn (Institute of Process Imaging) in collaboration with L. Schmidt, G. Brauckmann, V. Bueschler and A. Liese (Institute of Technical Biocatalalysis).

Enzyme immobilization enhances enzyme stability and recyclability for industrial use, but traditional quantification methods are slow, error-prone, and cannot assess enzymes inside pores. This study presents Time-Domain Nuclear Magnetic Resonance (TD-NMR) relaxometry as a non-invasive, direct technique to measure enzyme adsorption in porous epoxy methyl acrylate carriers. Changes in relaxation times correlate with enzyme concentration, enabling an NMR-based pore-filling ratio to quantify loading. TD-NMR results closely match traditional photometric data, providing a reliable and cost-effective alternative. The method is suitable for real-time monitoring and adaptable to various carriers and enzymes.

Highlights of this research:

  • Time-Domain NMR detects enzyme adsorption in porous carriers.
  • T2 relaxation times in porous carriers correlate with enzyme concentration.
  • An NMR pore-filling model links T2 relaxation times to enzyme loading.
  • Validation with epoxy methyl acrylate carriers agrees with photometric data.

M. Raquel Serial, Luca Schmidt, Muhammad Adrian, Grit Brauckmann, Stefan Benders, Victoria Bueschler, Andreas Liese, Alexander Penn (2026). A novel method for quantifying enzyme immobilization in porous carriers using simple NMR relaxometry. Biochemical Engineering Journal225, 109909.

https://doi.org/10.1016/j.bej.2025.109909.