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

Anal Bioanal Chem. 2006 May;385(1):146-52. doi: 10.1007/s00216-006-0398-1. Epub 2006 Apr 1.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzymes, Immobilized / chemistry*
  • Enzymes, Immobilized / metabolism
  • Glutamate Dehydrogenase / chemistry*
  • Glutamate Dehydrogenase / metabolism
  • Glutaral / chemistry
  • Glutaral / metabolism
  • Molecular Structure
  • Silicon Dioxide / chemistry*
  • Spectrometry, X-Ray Emission / methods*

Substances

  • Enzymes, Immobilized
  • Silicon Dioxide
  • Glutamate Dehydrogenase
  • Glutaral