Enzyme-catalysed siloxane bond formation
| Autor: | Alan R. Bassindale, Peter G. Taylor, Kurt Friedrich Brandstadt, Thomas H. Lane |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Siloxanes
medicine.medical_treatment Biochemistry Catalysis Inorganic Chemistry chemistry.chemical_compound Hydrolysis Biosynthesis Endopeptidases medicine Organic chemistry Silicic acid Lipase chemistry.chemical_classification Protease biology Chemistry Active site Silanes Silicon Dioxide Enzymes Kinetics Enzyme Siloxane biology.protein |
| Zdroj: | Journal of Inorganic Biochemistry. 96:401-406 |
| ISSN: | 0162-0134 |
| DOI: | 10.1016/s0162-0134(03)00177-6 |
| Popis: | 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 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. |
| Databáze: | OpenAIRE |
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