IEC 164 |
| Alan R. Bassindale1, Kurt F. Brandstadt2, Thomas H. Lane2, and Peter G. Taylor1. (1) Department of Chemistry, Open University, Milton Keynes, England, (2) Dow Corning Corporation, Midland, MI 48686 |
| 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 aurantia 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 performed to test the ability of enzymes to catalyze the formation of molecules with a single siloxane bond during the in vitro hydrolysis and condensation of alkoxysilanes. Our data suggests that homologous lipase and protease enzymes catalyze 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 catalyze the condensation of silanols. |
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General Poster Session
5:00 PM-7:00 PM, Tuesday, March 25, 2003 Convention Center -- Hall G, Poster
Sci-Mix
Division of Industrial and Engineering Chemistry |