Abbate, Vincenzo; Bassindale, Alan R.; Brandstadt, Kurt F.; Lawson, Rachel and Taylor, Peter G.
(2010).
| DOI (Digital Object Identifier) Link: | http://dx.doi.org/doi:10.1039/c0dt00151a |
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| Google Scholar: | Look up in Google Scholar |
Abstract
The potential for expanding the variety of enzymic methods for siloxane bond formation is explored. Three enzymes, Rhizopus oryzae lipase (ROL), lysozyme and phytase are reported to catalyse the condensation of the model compound, trimethylsilanol, formed in situ from trimethylethoxysilane, to produce hexamethyldisiloxane in aqueous media at 25 °C and pH 7. Thermal denaturation and reactant inhibition experiments were conducted to better understand the catalytic role of these enzyme candidates. It was found that enzyme activities were significantly reduced following thermal treatment, suggesting a potential key-role of the enzyme active sites in the catalysis. Similarly, residue-specific modification of the key-amino acids believed to participate in the ROL catalysis also had a significant effect on the silicon bio-catalysis, indicating that the catalytic triad of the lipase may be involved during the enzyme-mediated formation of the silicon–oxygen bond. E. coli phytase was found to be particularly effective at catalysing the condensation of trimethylsilanol in a predominantly organic medium consisting of 95% acetonitrile and 5% water. Whereas the use of enzymes in silicon chemistry is still very much a developing and frontier activity, the results presented herein give some grounds for optimism that the variety of enzyme mediated reactions will continue to increase and may one day become a routine element in the portfolio of the synthetic silicon chemist.
| Item Type: | Journal Article |
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| Copyright Holders: | 2010 RSC |
| ISSN: | 1477-9226 |
| Academic Unit/Department: | Other Departments > Other Departments Science > Life, Health and Chemical Sciences |
| Item ID: | 25700 |
| Depositing User: | Peter Taylor |
| Date Deposited: | 30 Dec 2010 14:24 |
| Last Modified: | 22 Nov 2012 17:12 |
| URI: | http://oro.open.ac.uk/id/eprint/25700 |
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