Enhanced Catalysis via Multiscale Force Propagation in All-Enzyme Glucose Oxidase Hydrogels
5 affiliations
- 1School of Physics and Astronomy
- 2University of Leeds
- 3Colorado State University
- 4ISIS Neutron and Muon Source
- 5Astbury Centre for Structural Molecular Biology
Abstract
Enzyme-based biomaterials are sustainable catalytic platforms with applications in biosensing, pharmaceutical synthesis, and environmental remediation. A key challenge is developing universal immobilisation strategies that preserve activity without requiring enzyme-specific optimisation. One promising approach is the photochemical cross-linking of native tyrosine residues to form self-supporting all-enzyme hydrogels, where the enzyme serves as both the catalytic and structural component. However, rational design of these materials requires understanding how gelation-induced forces propagate through the network and influence enzyme function. Here, we combine experiments and simulations to establish a multiscale framework linking hydrogel assembly, force propagation, and catalysis in glucose oxidase hydrogels. By varying the lamp intensity used during photochemical cross-linking, we control gelation kinetics and examine their consequences across molecular and network length scales. Slower gelation reduces enzyme unfolding and produces more loosely packed hydrogel networks with enhanced dynamic correlations and increased free volume around enzyme active sites. Integrating experimental measurements with modelling reveals that these structural changes enhance catalytic performance through altered force transmission across the network. Our findings demonstrate that enzyme activity is regulated not only by local active-site processes but also by collective mechanical interactions spanning multiple length scales, establishing network mechanics as a new design principle for functional biocatalytic materials.
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BibTeX
@misc{laurent2026enhanced,
title = {{Enhanced Catalysis via Multiscale Force Propagation in All-Enzyme Glucose Oxidase Hydrogels}},
author = {Harrison Laurent and Matt D. G. Hughes and Zoey Mikol and Ahmad Boroumand and Dimitra Katrantzi and Najet Mahmoudi and Marcelo C. R. Melo and Lorna Dougan},
howpublished = {ChemRxiv},
year = {2026},
month = oct,
doi = {10.26434/chemrxiv.15009743/v1},
url = {https://chemrxiv.org/doi/full/10.26434/chemrxiv.15009743/v1},
note = {CC BY-NC-ND},
}
RIS
TY - UNPB
TI - Enhanced Catalysis via Multiscale Force Propagation in All-Enzyme Glucose Oxidase Hydrogels
AU - Harrison Laurent
AU - Matt D. G. Hughes
AU - Zoey Mikol
AU - Ahmad Boroumand
AU - Dimitra Katrantzi
AU - Najet Mahmoudi
AU - Marcelo C. R. Melo
AU - Lorna Dougan
PY - 2026
DA - 2026/10/01
PB - ChemRxiv
DO - 10.26434/chemrxiv.15009743/v1
UR - https://chemrxiv.org/doi/full/10.26434/chemrxiv.15009743/v1
AB - Enzyme-based biomaterials are sustainable catalytic platforms with applications in biosensing, pharmaceutical synthesis, and environmental remediation. A key challenge is developing universal immobilisation strategies that preserve activity without requiring enzyme-specific optimisation. One promising approach is the photochemical cross-linking of native tyrosine residues to form self-supporting all-enzyme hydrogels, where the enzyme serves as both the catalytic and structural component. However, rational design of these materials requires understanding how gelation-induced forces propagate through the network and influence enzyme function. Here, we combine experiments and simulations to establish a multiscale framework linking hydrogel assembly, force propagation, and catalysis in glucose oxidase hydrogels. By varying the lamp intensity used during photochemical cross-linking, we control gelation kinetics and examine their consequences across molecular and network length scales. Slower gelation reduces enzyme unfolding and produces more loosely packed hydrogel networks with enhanced dynamic correlations and increased free volume around enzyme active sites. Integrating experimental measurements with modelling reveals that these structural changes enhance catalytic performance through altered force transmission across the network. Our findings demonstrate that enzyme activity is regulated not only by local active-site processes but also by collective mechanical interactions spanning multiple length scales, establishing network mechanics as a new design principle for functional biocatalytic materials.
ER -