Protein Self-Assembly as a Design Principle for Enzyme Immobilisation in Biocatalysis
- 1School of Natural Sciences, Macquarie University, Sydney, NSW 2109, Australia
- 2Australian Research Council Industrial Transformation Training Centre for Facilitated Advancement of Australia’s Bioactives (FAAB), Sydney, NSW 2109, Australia
Abstract
Enzyme immobilisation is essential for translating biocatalytic processes from the laboratory to industrial applications by improving enzyme stability, recovery, and reuse. It underpins sustainable processes in pharmaceuticals, biofuels, and food production, but conventional immobilisation strategies involve inherent trade-offs. Covalent attachment prevents enzyme leaching but may distort the active site, whereas physical adsorption better preserves enzyme conformation but allows enzyme leaching. Furthermore, carrier-based methods frequently encounter mass-transfer limitations and may require external cross-linkers, hindering broader industrial application. Recent advances in synthetic biology and materials science have accelerated the development of protein-based materials for biocatalysis. This review examines protein self-assembly as a unifying design principle for enzyme immobilisation, enabling programmable assembly under relatively mild conditions to overcome key limitations of conventional strategies. We discuss naturally derived structures such as bacterial microcompartments and engineered systems including virus-like particles, elastin-like polypeptides, and SpyTag/SpyCatcher, which support programmable enzyme organisation and enable compartmentalised multi-enzyme cascade reactions. Building on this, a major focus is placed on catalytically active inclusion bodies (CatIBs). As robust, intrinsically self-immobilised protein aggregates, CatIBs represent a simplified, carrier-free platform offering potential process and cost advantages for industrial biocatalysis.
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BibTeX
@article{vijayakumar2026protein,
title = {{Protein Self-Assembly as a Design Principle for Enzyme Immobilisation in Biocatalysis}},
author = {Santhosh Vijayakumar and Anwar Sunna},
journal = {International Journal of Molecular Sciences},
year = {2026},
month = oct,
doi = {10.3390/ijms27209187},
url = {https://www.mdpi.com/1422-0067/27/20/9187},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Protein Self-Assembly as a Design Principle for Enzyme Immobilisation in Biocatalysis
AU - Santhosh Vijayakumar
AU - Anwar Sunna
PY - 2026
DA - 2026/10/01
JO - International Journal of Molecular Sciences
DO - 10.3390/ijms27209187
UR - https://www.mdpi.com/1422-0067/27/20/9187
AB - Enzyme immobilisation is essential for translating biocatalytic processes from the laboratory to industrial applications by improving enzyme stability, recovery, and reuse. It underpins sustainable processes in pharmaceuticals, biofuels, and food production, but conventional immobilisation strategies involve inherent trade-offs. Covalent attachment prevents enzyme leaching but may distort the active site, whereas physical adsorption better preserves enzyme conformation but allows enzyme leaching. Furthermore, carrier-based methods frequently encounter mass-transfer limitations and may require external cross-linkers, hindering broader industrial application. Recent advances in synthetic biology and materials science have accelerated the development of protein-based materials for biocatalysis. This review examines protein self-assembly as a unifying design principle for enzyme immobilisation, enabling programmable assembly under relatively mild conditions to overcome key limitations of conventional strategies. We discuss naturally derived structures such as bacterial microcompartments and engineered systems including virus-like particles, elastin-like polypeptides, and SpyTag/SpyCatcher, which support programmable enzyme organisation and enable compartmentalised multi-enzyme cascade reactions. Building on this, a major focus is placed on catalytically active inclusion bodies (CatIBs). As robust, intrinsically self-immobilised protein aggregates, CatIBs represent a simplified, carrier-free platform offering potential process and cost advantages for industrial biocatalysis.
SN - 1422-0067
ER -