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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

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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.

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Acknowledgements

The authors acknowledge MIUR for financial support and CIS (University of Bari, Bari, Italy) for XPS measurements. The authors thank also University of Lecce (Lecce, Italy) and Consorzio INCA (Venice, Italy) for their support.

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Authors and Affiliations

  1. Dipartimento di Ingegneria dell’Innovazione, Università di Lecce, via Arnesano, 73100, Lecce, Italy

    Luigia Longo & Giuseppe Vasapollo

  2. Dipartimento di Scienza dei Materiali, Università di Lecce, via Arnesano, 73100, Lecce, Italy

    Maria Rachele Guascito & Cosimino Malitesta

Authors
  1. Luigia Longo
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  2. Giuseppe Vasapollo
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  3. Maria Rachele Guascito
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  4. Cosimino Malitesta
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Correspondence to Cosimino Malitesta.

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Longo, L., Vasapollo, G., Guascito, M.R. et al. 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 385, 146–152 (2006). https://doi.org/10.1007/s00216-006-0398-1

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  • DOI: https://doi.org/10.1007/s00216-006-0398-1

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