ArticleChemSusChem2022
Polar Substitutions on the Surface of a Lipase Substantially Improve Tolerance in Organic Solvents.
Article in ChemSusChem, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 38 citations in OpenAlex.
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- Recent advances on protein engineering for improved stability.Biodesign research · 2025Review
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- Article
- Solvent Tolerance Improvement of Lipases Enhanced Their Applications: State of the Art.Molecules (Basel, Switzerland) · 2024Review
- Engineering diaryl alcohol dehydrogenase KpADH reveals importance of retaining hydration shell in organic solvent tolerance.Protein science : a publication of the Protein Society · 2024Article
- Enhanced Activity and Stability of an Acetyl Xylan Esterase in Hydrophilic Alcohols through Site-Directed Mutagenesis.Molecules (Basel, Switzerland) · 2023Article
- Cationic Polymers Remarkably Boost Haloalkane Dehalogenase Activity in Organic Solvent Solutions and the Molecular Implications.Molecules (Basel, Switzerland) · 2023Article
- Engineering aRSC advances · 2023Article
- Polar Substitutions on the Surface of a Lipase Substantially Improve Tolerance in Organic Solvents.ChemSusChem · 2022Article
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Authors and funding
6 authors at 6 institutions in 3 countries.
Funding
Abstract
Biocatalysis in organic solvents (OSs) enables more efficient routes to the synthesis of various valuable chemicals. However, OSs often reduce enzymatic activity, which limits the use of enzymes in OSs. Herein, we report a comprehensive understanding of interactions between surface polar substitutions and DMSO by integrating molecular dynamics (MD) simulations of 45 variants from Bacillus subtilis lipase A (BSLA) and substitution landscape into a "BSLA-SSM" library. By systematically analyzing 39 structural-, solvation-, and interaction energy-based observables, we discovered that hydration shell maintenance, DMSO reduction, and decreased local flexibility simultaneously govern the stability of polar variants in OS. Moreover, the fingerprints of 1631 polar-related variants in three OSs demonstrated that substituting aromatic to polar amino acid(s) hold great potential to highly improve OSs resistance. Hence, surface polar engineering is a powerful strategy to generate OS-tolerant lipases and other enzymes, thereby adapting the catalyst to the desired reaction and process with OSs.
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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.