Matches in SemOpenAlex for { <https://semopenalex.org/work/W2891621933> ?p ?o ?g. }
- W2891621933 abstract "Enzymatic synthesis in organic solvents holds increasing industrial opportunities in many fields; however, one major obstacle is the limited stability of biocatalysts in such a denaturing environment. Aromatic interactions play a major role in protein folding and stability, and we were inspired by this to redesign enzyme voids. The rational protein engineering of solvent tunnels of lipase from Geobacillus stearothermophilus is presented here, offering a promising approach to introduce new aromatic interactions within the enzyme core. We discovered that longer tunnels leading from the surface to the enzyme active site were more beneficial targets for mutagenesis for improving lipase stability in methanol during biodiesel biosynthesis. A structural analysis of the variants confirmed the generation of new interactions involving aromatic residues. This work provides insights into stability-driven enzyme design by targeting the solvent channel void." @default.
- W2891621933 created "2018-09-27" @default.
- W2891621933 creator A5033869343 @default.
- W2891621933 creator A5049605110 @default.
- W2891621933 creator A5049946053 @default.
- W2891621933 creator A5055437472 @default.
- W2891621933 date "2018-12-01" @default.
- W2891621933 modified "2023-10-16" @default.
- W2891621933 title "Filling the Void: Introducing Aromatic Interactions into Solvent Tunnels To Enhance Lipase Stability in Methanol" @default.
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- W2891621933 doi "https://doi.org/10.1128/aem.02143-18" @default.