Supra-biological performance of immobilized enzymes enabled by chaperone-like specific non-covalent interactions

Héctor Sánchez-Morán, Joel L. Kaar () and Daniel K. Schwartz ()
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Héctor Sánchez-Morán: University of Colorado Boulder
Joel L. Kaar: University of Colorado Boulder
Daniel K. Schwartz: University of Colorado Boulder

Nature Communications, 2024, vol. 15, issue 1, 1-12

Abstract: Abstract Designing complex synthetic materials for enzyme immobilization could unlock the utility of biocatalysis in extreme environments. Inspired by biology, we investigate the use of random copolymer brushes as dynamic immobilization supports that enable supra-biological catalytic performance of immobilized enzymes. This is demonstrated by immobilizing Bacillus subtilis Lipase A on brushes doped with aromatic moieties, which can interact with the lipase through multiple non-covalent interactions. Incorporation of aromatic groups leads to a 50 °C increase in the optimal temperature of lipase, as well as a 50-fold enhancement in enzyme activity. Single-molecule FRET studies reveal that these supports act as biomimetic chaperones by promoting enzyme refolding and stabilizing the enzyme’s folded and catalytically active state. This effect is diminished when aromatic residues are mutated out, suggesting the importance of π-stacking and π-cation interactions for stabilization. Our results underscore how unexplored enzyme-support interactions may enable uncharted opportunities for using enzymes in industrial biotransformations.

Date: 2024
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DOI: 10.1038/s41467-024-46719-5

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