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Grafted-from Polymer Surface Display: A Platform for In Situ Engineering of Robust and Recoverable Biocatalysts
Wen Zhou1, Felizitas Suhm1, Henrik Karring2
1Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230 Odense, Denmark.
Biomacromolecules
|June 19, 2026
Summary
We developed a novel surface display method to grow polymers directly on enzymes, enhancing their stability and enabling easy recovery. This creates robust, self-recovering biocatalysts without complex purification.
Area of Science:
- Biotechnology
- Polymer Chemistry
- Enzyme Engineering
Background:
- Protein-polymer conjugation and microbial surface display are key enzyme engineering strategies.
- These methods face limitations in purification and stability.
- Existing approaches have evolved separately, hindering synergistic advancements.
Purpose of the Study:
- To introduce a "grafted-from surface display" platform integrating protein engineering and polymer chemistry.
- To enable in situ polymerization on surface-displayed proteins without purification.
- To create robust, self-recovering biocatalysts with enhanced stability and simplified recovery.
Main Methods:
- Utilized *Escherichia coli* displaying cysteine-engineered benzaldehyde lyase (sBALS174C).
- Performed in situ atom transfer radical polymerization (ATRP) to grow thermoresponsive poly(N-isopropylacrylamide) (PNIPAM) polymers.
- Assessed enzyme activity, stability at elevated temperatures, and recyclability in a multienzyme cascade.
Main Results:
- PNIPAM grafting significantly enhanced enzyme robustness, retaining >60% activity at 50 °C.
- The modified enzymes showed temperature-controlled recovery and purification via centrifugation.
- A multienzyme cascade achieved 15 mM benzoin yield and >80% activity after four cycles.
Conclusions:
- Grafted-from surface display provides a facile framework for creating robust, self-recovering biocatalysts.
- This approach integrates synthetic polymer chemistry with cellular machinery, bypassing laborious protein isolation.
- The method enhances enzyme stability and simplifies recovery, offering a significant advancement in biocatalysis.
