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New insights from X-ray photoelectron spectroscopy into the chemistry of covalent enzyme immobilization, with glutamate dehydrogenase (GDH) on silicon dioxide as an example
Authors:Luigia Longo  Giuseppe Vasapollo  Maria Rachele Guascito  Cosimino Malitesta
Affiliation:(1) Dipartimento di Ingegneria dell’Innovazione, Università di Lecce, via Arnesano, 73100 Lecce, Italy;(2) Dipartimento di Scienza dei Materiali, Università di Lecce, via Arnesano, 73100 Lecce, Italy
Abstract: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.
Keywords:X-ray photoelectron spectroscopy  Glutamate dehydrogenase  Enzyme covalent immobilization  Silicon dioxide
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