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 |
本文献已被 PubMed SpringerLink 等数据库收录! |
|