ArticleNature communications2024
Supra-biological performance of immobilized enzymes enabled by chaperone-like specific non-covalent interactions.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 30 citations in OpenAlex.
- Enhancing Enzyme Activity Via Noncovalent Association with DNA-Functionalized Nanoparticles.JACS Au · 2026Article
- Targeting biofilm and virulence inMicrobiology spectrum · 2026Article
- Changes in the pH-Activity Profiles of Enzymes upon Immobilization on Polyelectrolyte-Containing Hydrogels.Chem & bio engineering · 2026Article
- Smart Hydrogel Doped by Metal-Organic Frameworks for Renewable Self-Pumping Enzymatic Reactors.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Discovery of Surface-Engineered Nanoparticles That Boost Enzyme Activity via High-Throughput Screening and Machine Learning.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Enhanced enzyme stability at the interphase of water-oil for continuous-flow olefin epoxidation.Nature communications · 2025Article
- Surface-Engineered Nanoparticles Enhance the Peroxidase Activity of Heme-Containing Proteins.ACS nano · 2025Article
- Keeping the Distance: Activity Control in Solid-Supported Sucrose Phosphorylase by a Rigid α-Helical Linker of Tunable Spacer Length.ACS catalysis · 2024Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.