Polar Substitutions on the Surface of a Lipase Substantially Improve Tolerance in Organic Solvents
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.
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
Polar Substitutions on the Surface of a Lipase Substantially Improve Tolerance in Organic Solvents ; day:09 ; month:02 ; year:2022 ; extent:1
ChemSusChem ; (09.02.2022) (gesamt 1)
- Creator
- DOI
-
10.1002/cssc.202102551
- URN
-
urn:nbn:de:101:1-2022020914422341258493
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:21 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Cui, Haiyang
- Vedder, Markus
- Zhang, Lingling
- Jaeger, Karl‐Erich
- Schwaneberg, Ulrich
- Davari, Mehdi D.
Other Objects (12)
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Engineering of Laccase CueO for Improved Electron Transfer in Bioelectrocatalysis by Semi‐Rational Design
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Engineering of Laccase CueO for Improved Electron Transfer in Bioelectrocatalysis by Semi-Rational Design
CompassR Yields Highly Organic‐Solvent‐Tolerant Enzymes through Recombination of Compatible Substitutions
Lipase‐Mediated Conversion of Protecting Group Silyl Ethers: An Unspecific Side Reaction
Local existence and uniqueness of increasing positive solutions for non-singular and singular beam equation with a parameter
Existence of positive solutions of boundary value problems for high-order nonlinear conformable differential equations with p-Laplacian operator
Local existence–uniqueness and monotone iterative approximation of positive solutions for p-Laplacian differential equations involving tempered fractional derivatives
Existence and uniqueness of positive solutions for a class of nonlinear fractional differential equations
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Engineering of Laccase CueO for Improved Electron Transfer in Bioelectrocatalysis by Semi‐Rational Design
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Engineering of Laccase CueO for Improved Electron Transfer in Bioelectrocatalysis by Semi-Rational Design
CompassR Yields Highly Organic‐Solvent‐Tolerant Enzymes through Recombination of Compatible Substitutions
Lipase‐Mediated Conversion of Protecting Group Silyl Ethers: An Unspecific Side Reaction
Local existence and uniqueness of increasing positive solutions for non-singular and singular beam equation with a parameter
Existence of positive solutions of boundary value problems for high-order nonlinear conformable differential equations with p-Laplacian operator
Local existence–uniqueness and monotone iterative approximation of positive solutions for p-Laplacian differential equations involving tempered fractional derivatives
Existence and uniqueness of positive solutions for a class of nonlinear fractional differential equations
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Engineering of Laccase CueO for Improved Electron Transfer in Bioelectrocatalysis by Semi‐Rational Design
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Engineering of Laccase CueO for Improved Electron Transfer in Bioelectrocatalysis by Semi-Rational Design
CompassR Yields Highly Organic‐Solvent‐Tolerant Enzymes through Recombination of Compatible Substitutions
Lipase‐Mediated Conversion of Protecting Group Silyl Ethers: An Unspecific Side Reaction
Local existence and uniqueness of increasing positive solutions for non-singular and singular beam equation with a parameter
Existence of positive solutions of boundary value problems for high-order nonlinear conformable differential equations with p-Laplacian operator
Local existence–uniqueness and monotone iterative approximation of positive solutions for p-Laplacian differential equations involving tempered fractional derivatives