ArticleNature communications2024
Solvent concentration at 50% protein unfolding may reform enzyme stability ranking and process window identification.
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 5 papers.
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Who cites it
5 citing papers in PubMed.
- Multigram-Scale Asymmetric Alkene Reduction Catalyzed by a Thermostable Flavin Ene-Reductase.Organic process research & development · 2026Article
- Cold-adapted carboxylesterases from Alcanivoracaceae active with a wide range of synthetic polyesters.Applied microbiology and biotechnology · 2026Article
- A Computational Perspective to Intermolecular Interactions and the Role of the Solvent on Regulating Protein Properties.Chemical reviews · 2025Review
- Recent advances on protein engineering for improved stability.Biodesign research · 2025Review
- Solvent concentration at 50% protein unfolding may reform enzyme stability ranking and process window identification.Nature communications · 2024Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As water miscible organic co-solvents are often required for enzyme reactions to improve e.g., the solubility of the substrate in the aqueous medium, an enzyme is required which displays high stability in the presence of this co-solvent. Consequently, it is of utmost importance to identify the most suitable enzyme or the appropriate reaction conditions. Until now, the melting temperature is used in general as a measure for stability of enzymes. The experiments here show, that the melting temperature does not correlate to the activity observed in the presence of the solvent. As an alternative parameter, the concentration of the co-solvent at the point of 50% protein unfolding at a specific temperature T in short
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