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    •   UVaDOC Startseite
    • WISSENSCHAFTLICHE ARBEITEN
    • Departamentos
    • Dpto. Química Física y Química Inorgánica
    • DEP63 - Artículos de revista
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    Por favor, use este identificador para citar o enlazar este ítem:http://uvadoc.uva.es/handle/10324/30702

    Título
    Advantages of the biomimetic nanostructured films as an immobilization method vs. the carbon paste classical method
    Autor
    Rodríguez Méndez, María LuzAutoridad UVA Orcid
    Apetrei, Constantin
    Saja Saez, José Antonio DeAutoridad UVA Orcid
    Zurro Hernández, Luis JavierAutoridad UVA
    Año del Documento
    2012
    Documento Fuente
    Catalysts vol. 2 p. 517-531
    Zusammenfassung
    Tyrosinase-based biosensors containing a phthalocyanine as electron mediator have been prepared by two different methods. In the first approach, the enzyme and the electron mediator have been immobilized in carbon paste electrodes. In the second method, they have been introduced in an arachidic acid Langmuir-Blodgett nanostructured film that provides a biomimetic environment. The sensing properties of non-nanostructured and nanostructured biosensors towards catechol, catechin and phenol have been analyzed and compared. The enzyme retains the biocatalytic properties in both matrixes. However, the nanostructured biomimetic films show higher values of maximum reaction rates and lowest apparent Michaelis-Menten constants. In both types of sensors, the sensitivity follows the decreasing order catechol > catechin > phenol. The detection limits observed are in the range of 1.8–5.4 μM for Langmuir-Blodgett biosensors and 8.19–8.57 μM for carbon paste biosensors. In summary, it has been demonstrated that the Langmuir-Blodgett films provide a biomimetic environment and nanostructured biosensors show better performances in terms of kinetic, detection limit and stability.
    ISSN
    2073-4344
    Revisión por pares
    SI
    DOI
    10.3390/catal2040517
    Idioma
    eng
    URI
    http://uvadoc.uva.es/handle/10324/30702
    Derechos
    openAccess
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    • DEP63 - Artículos de revista [324]
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    Universidad de Valladolid

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