Abstract
Using the sol-gel process, the enzyme glucose-oxidase was immobilized in modified SiO2 layers. The tetraethoxysilane based sol was varied by veratrylaldehyde, aminopropyltriethoxysilane and an azomethine compound, which was synthesized from both molecules. Changes in reaction kinetics of the sol-gel process by addition of veratrylaldehyde were observed by 29Si NMR measurements. The fixation of this additive in the final gel was clarified by FTIR spectroscopy.
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