Biocatalytic Silylation: The Condensation of Phenols and Alcohols with Triethylsilanol
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 sub...
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MDPI AG
2021-07-01
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| Online Access: | https://www.mdpi.com/2073-4344/11/8/879 |
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| author | Emily I. Sparkes Chisom S. Egedeuzu Billie Lias Rehana Sung Stephanie A. Caslin S. Yasin Tabatabaei Dakhili Peter G. Taylor Peter Quayle Lu Shin Wong |
| author_facet | Emily I. Sparkes Chisom S. Egedeuzu Billie Lias Rehana Sung Stephanie A. Caslin S. Yasin Tabatabaei Dakhili Peter G. Taylor Peter Quayle Lu Shin Wong |
| author_sort | Emily I. Sparkes |
| collection | DOAJ |
| description | 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 <i>S</i>-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 <i>n</i>-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. |
| first_indexed | 2024-03-10T08:56:20Z |
| format | Article |
| id | doaj.art-38ca50e7ce5549f8ace1fafae3935208 |
| institution | Directory Open Access Journal |
| issn | 2073-4344 |
| language | English |
| last_indexed | 2024-03-10T08:56:20Z |
| publishDate | 2021-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Catalysts |
| spelling | doaj.art-38ca50e7ce5549f8ace1fafae39352082023-11-22T07:06:07ZengMDPI AGCatalysts2073-43442021-07-0111887910.3390/catal11080879Biocatalytic Silylation: The Condensation of Phenols and Alcohols with TriethylsilanolEmily I. Sparkes0Chisom S. Egedeuzu1Billie Lias2Rehana Sung3Stephanie A. Caslin4S. Yasin Tabatabaei Dakhili5Peter G. Taylor6Peter Quayle7Lu Shin Wong8Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UKManchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UKManchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UKManchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UKManchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UKManchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UKFaculty of Science, Technology, Engineering and Mathematics, Open University, Walton Hall, Milton Keynes MK7 6AA, UKDepartment of Chemistry, University of Manchester, Oxford Road, Manchester M13 9PL, UKManchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UKSilicatein-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 <i>S</i>-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 <i>n</i>-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.https://www.mdpi.com/2073-4344/11/8/879silicateincondensationsilyl etherorganosiloxanesbiocatalysis |
| spellingShingle | Emily I. Sparkes Chisom S. Egedeuzu Billie Lias Rehana Sung Stephanie A. Caslin S. Yasin Tabatabaei Dakhili Peter G. Taylor Peter Quayle Lu Shin Wong Biocatalytic Silylation: The Condensation of Phenols and Alcohols with Triethylsilanol Catalysts silicatein condensation silyl ether organosiloxanes biocatalysis |
| title | Biocatalytic Silylation: The Condensation of Phenols and Alcohols with Triethylsilanol |
| title_full | Biocatalytic Silylation: The Condensation of Phenols and Alcohols with Triethylsilanol |
| title_fullStr | Biocatalytic Silylation: The Condensation of Phenols and Alcohols with Triethylsilanol |
| title_full_unstemmed | Biocatalytic Silylation: The Condensation of Phenols and Alcohols with Triethylsilanol |
| title_short | Biocatalytic Silylation: The Condensation of Phenols and Alcohols with Triethylsilanol |
| title_sort | biocatalytic silylation the condensation of phenols and alcohols with triethylsilanol |
| topic | silicatein condensation silyl ether organosiloxanes biocatalysis |
| url | https://www.mdpi.com/2073-4344/11/8/879 |
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