Bassindale, Alan R.; Brandstadt, Kurt F.; Lane, Thomas H. and Taylor, Peter G.
|DOI (Digital Object Identifier) Link:||http://dx.doi.org/10.1016/S0162-0134(03)00177-6|
|Google Scholar:||Look up in Google Scholar|
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|
|Keywords:||Lipase; Protease; Hydrolysis; Condensation; Siloxane bond|
|Academic Unit/Department:||Other Departments > Other Departments
Science > Life, Health and Chemical Sciences
|Interdisciplinary Research Centre:||Centre for Earth, Planetary, Space and Astronomical Research (CEPSAR)
|Depositing User:||Peter Taylor|
|Date Deposited:||04 Jul 2006|
|Last Modified:||05 Mar 2014 10:39|
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