http://www.cnr.it/ontology/cnr/individuo/prodotto/ID36047
Layer uniformity in glucose oxidase immobilization on SiO2 surfaces (Articolo in rivista)
- Type
- Label
- Layer uniformity in glucose oxidase immobilization on SiO2 surfaces (Articolo in rivista) (literal)
- Anno
- 2007-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.apsusc.2007.05.039 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Libertino S; Scandurra A; Aiello V; Giannazzo F; Sinatra F; Renis M; Fichera M (literal)
- Pagina inizio
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- IMM-CNR, I-95121 Catania, Italy;
Consorzio Catania Ric, Lab Superfici & Interfasi SUPERLAB, I-95121 Catania, Italy;
Catania Univ, Dipartimento Chim Biol Chim Med & Biol Mol, I-95121 Catania, Italy;
Univ Catania, Dipartimento Sci Biomed, I-95100 Catania, Italy (literal)
- Titolo
- Layer uniformity in glucose oxidase immobilization on SiO2 surfaces (literal)
- Abstract
- The goal of this work was the characterization, step by step, of the enzyme glucose oxidase (GOx) immobilization on silicon oxide surfaces, mainly by means of X-Ray photoelectron spectroscopy (XPS). The immobilization protocol consists of four steps: oxide activation, silanization, linker molecule deposition and GOx immobilization. The linker molecule, glutaraldehyde (GA) in this study, must be able to form a uniform layer on the sample surface in order to maximize the sites available for enzyme bonding and achieve the best enzyme deposition. Using a thin SiO2 layer crown on Si wafers and following the XPS Si2p signal of the Si substrate during the immobilization steps, we demonstrated both the glutaraldehyde layer uniformity and the possibility to use XPS to monitor thin layer uniformity. In fact, the XPS substrate signal, not shielded by the oxide, is suppressed only when a uniform layer is deposited. The enzyme correct immobilization was monitored using the XPS C1s and N1s signals. Atomic force microscopy (AFM) measurements carried out on the same samples confirmed the results. (literal)
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