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Enzyme-catalysed siloxane bond formation

Bassindale, Alan R.; Brandstadt, Kurt F.; Lane, Thomas H. and Taylor, Peter G. (2003). Enzyme-catalysed siloxane bond formation. Journal of Inorganic Biochemistry, 96(2-3) pp. 401–406.

DOI (Digital Object Identifier) Link: https://doi.org/10.1016/S0162-0134(03)00177-6
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Abstract

Biosilicification occurs on a globally vast scale under mild conditions. Although research has progressed in the area of silica biosynthesis, the molecular mechanisms of these interactions are effectively unknown. The natural production of silica in the Tethya urantia marine sponge, Cylindrotheca fusiformis diatom, and Equisetum telmateia plant appear to be similar. However, the studies were
complicated mechanistic queries due to the use of silicic acid analogues. Given these complications, a carefully chosen model study was carried out to test the ability of enzymes to catalyse the formation of molecules with a single siloxane bond during the in vitro hydrolysis and condensation of alkoxysilanes. Our data suggest that homologous lipase and protease enzymes catalyse the formation of siloxane bonds under mild conditions. Non-specific interactions with trypsin promoted the in vitro hydrolysis of alkoxysilanes, while the active site was determined to selectively catalyse the condensation of silanols.

Item Type: Journal Article
ISSN: 0162-0134
Keywords: Lipase; Protease; Hydrolysis; Condensation; Siloxane bond
Academic Unit/School: Other Departments > Vice-Chancellor's Office
Other Departments
Faculty of Science, Technology, Engineering and Mathematics (STEM) > Life, Health and Chemical Sciences
Faculty of Science, Technology, Engineering and Mathematics (STEM)
Interdisciplinary Research Centre: Biomedical Research Network (BRN)
Centre for Earth, Planetary, Space and Astronomical Research (CEPSAR)
Item ID: 4025
Depositing User: Peter Taylor
Date Deposited: 04 Jul 2006
Last Modified: 30 Nov 2016 14:34
URI: http://oro.open.ac.uk/id/eprint/4025
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