Biocatalytic Silylation: The Condensation of Phenols and Alcohols with Triethylsilanol

Emily I. Sparkes, Chisom Egedeuzu, Billie Lias, Rehana Sung, Stephanie A. Caslin, S. Yasin Tabatabaei Dakhili, Peter G. Taylor, Peter Quayle, Lu Shin Wong

Research output: Contribution to journalArticlepeer-review

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

Research Beacons, Institutes and Platforms

  • Manchester Institute of Biotechnology

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