New insights from X-ray photoelectron spectroscopy into the chemistry of covalent enzyme immobilization, with glutamate dehydrogenase (GDH) on silicon dioxide as an example

A three-step process for immobilization of glutamate dehydrogenase (GDH) on the surface of silicon dioxide has been studied by X-ray photoelectron spectroscopy (XPS). The enzyme layer was deposited on the silicon dioxide surface after first exposing the surface to 3-aminopropyltriethoxysilane (3-APT...

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Bibliographic Details
Published in:Analytical and bioanalytical chemistry 2006-05, Vol.385 (1), p.146-152
Main Authors: Longo, Luigia, Vasapollo, Giuseppe, Guascito, Maria Rachele, Malitesta, Cosimino
Format: Article
Language:English
Subjects:
Aminopropyltriethoxysilane
Dehydrogenase
Dehydrogenases
Enzyme covalent immobilization
Enzymes
Enzymes, Immobilized - chemistry
Enzymes, Immobilized - metabolism
Glutamate dehydrogenase
Glutamate Dehydrogenase - chemistry
Glutamate Dehydrogenase - metabolism
Glutaral - chemistry
Glutaral - metabolism
Immobilization
Molecular Structure
Photoelectron spectroscopy
Photoelectrons
Silica
Silicon
Silicon dioxide
Silicon Dioxide - chemistry
Spectrometry, X-Ray Emission - methods
Spectroscopy
X ray photoelectron spectroscopy
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Summary:A three-step process for immobilization of glutamate dehydrogenase (GDH) on the surface of silicon dioxide has been studied by X-ray photoelectron spectroscopy (XPS). The enzyme layer was deposited on the silicon dioxide surface after first exposing the surface to 3-aminopropyltriethoxysilane (3-APTS) and reacting the silylated surface with glutaraldehyde (GA). Fine XPS analysis, performed after each step of the chemical procedure, revealed unknown details of the step-by-step construction of the enzyme layer under different experimental conditions.
ISSN:1618-2642
1618-2650
DOI:10.1007/s00216-006-0398-1