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

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

SUBMITTER: Sanchez-Moran H 

PROVIDER: S-EPMC10940687 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature