Biocatalytic Silylation: The Condensation of Phenols and Alcohols with Triethylsilanol

Research output: Contribution to journalArticlepeer-review

  • External authors:
  • Emily I. Sparkes
  • Billie Lias
  • Rehana Sung
  • Stephanie A. Caslin
  • S. Yasin Tabatabaei Dakhili
  • Peter G. Taylor

Abstract

Silicatein-α (Silα), a hydrolytic enzyme derived from siliceous marine sponges, is one of the few enzymes in nature capable of catalysing the metathesis of silicon–oxygen bonds. It is therefore of interest as a possible biocatalyst for the synthesis of organosiloxanes. To further investigate the substrate scope of this enzyme, a series of condensation reactions with a variety of phenols and aliphatic alcohols were carried out. In general, it was observed that Silα demonstrated a preference for phenols, though the conversions were relatively modest in most cases. In the two pairs of chiral alcohols that were investigated, it was found that the enzyme displayed a preference for the silylation of the S-enantiomers. Additionally, the enzyme’s tolerance to a range of solvents was tested. Silα had the highest level of substrate conversion in the nonpolar solvents n-octane and toluene, although the inclusion of up to 20% of 1,4-dioxane was tolerated. These results suggest that Silα is a potential candidate for directed evolution toward future application as a robust and selective biocatalyst for organosiloxane chemistry.

Bibliographical metadata

Original languageEnglish
Article number879
JournalCatalysts
Volume11
Issue number8
DOIs
Publication statusPublished - 22 Jul 2021

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