NDLI: Enzyme-mediated Synthesis of Silsesquioxanes

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Enzyme-mediated Synthesis of Silsesquioxanes

Content Provider	Springer Nature Link
Author	Frampton, Mark Simionescu, Razvan Zelisko, Paul M.
Copyright Year	2009
Abstract	In an initial report we demonstrated that some serine proteases were suitable candidates for the hydrolysis and condensation of tetraethoxysilane and phenyltrimethoxysilane under solvent-free conditions. Using trypsin as a model enzyme, we have demonstrated the generality of this method by expanding the number of available silicon-based substrates that can be processed by the enzyme, as well as including pepsin to demonstrate that this phenomenon is not exclusive to a single family of enzymes. A series of time course $^{29}$Si NMR experiments using D$_{2}$O revealed that the rate of hydrolysis of phenyltrimethoxysilane could be enhanced by a factor of 11–155 times over enzyme-free controls when either trypsin or pepsin were used as catalysts. The following trend was observed when comparing the hydrolysis/condensation rates of a number of different organotrimethoxysilanes: methyltrimethoxysilane>allytrimethoxysilane>ethyltrimethoxysilane>phenyltrimethoxysilane.
Starting Page	47
Ending Page	56
Page Count	10
File Format	PDF
ISSN	1876990X
Journal	Silicon
Volume Number	1
Issue Number	1
e-ISSN	18769918
Language	English
Publisher	Springer Netherlands
Publisher Date	2009-02-20
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biocatalysis Silicon NMR Siloxane bond Organotrialkoxysilane Silsesquioxane Enzyme-mediated Nanotechnology Biomedical Engineering Polymer Sciences Organic Chemistry Materials Science Inorganic Chemistry
Content Type	Text
Resource Type	Article
Subject	Electronic, Optical and Magnetic Materials

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