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-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.
Dipartimento di Ingegneria dell'Innovazione, Università di Lecce, via Arnesano, 73100 Lecce, Italy.
Luigia
L
Longo
Giuseppe
G
Vasapollo
Maria Rachele
MR
Guascito
Cosimino
C
Malitesta
D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism; D005969:Glutamate Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D005976:Glutaral / Q000737:chemistry / Q000378:metabolism; D015394:Molecular Structure; D012822:Silicon Dioxide / Q000737:chemistry*; D013052:Spectrometry, X-Ray Emission / Q000379:methods*
D004800:Enzymes, Immobilized; D012822:Silicon Dioxide; D005969:Glutamate Dehydrogenase; D005976:Glutaral