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Title

Laccase biosensors based on different enzyme immobilization strategies for phenolic compounds determination

AuthorsCasero, Elena; Petit-Domínguez, M. Dolores; Vázquez, Luis ; Ramírez-Asperilla, I.; Parra-Alfambra, A. M.; Pariente, F.; Lorenzo, Encarnación
KeywordsAtomic force microscopy
Enzyme immobilization
Amperometric biosensors
Phenolic compounds
Trametes versicolor laccase
Issue Date2013
PublisherElsevier
CitationTalanta 115: 401-408 (2013)
AbstractDifferent enzyme immobilization approaches of Trametes versicolor laccase (TvL) onto gold surfaces and their influence on the performance of the final bioanalytical platforms are described. The laccase immobilization methods include: (i) direct adsorption onto gold electrodes (TvL/Au), (ii) covalent attachment to a gold surface modified with a bifunctional reagent, 3,3'-Dithiodipropionic acid di (N-succinimidyl ester) (DTSP), and (iii) integration of the enzyme into a sol-gel 3D polymeric network derived from (3-mercaptopropyl)-trimethoxysilane (MPTS) previously formed onto a gold surface (TvL/MPTS/Au). The characterization and applicability of these biosensors are described. Characterization is performed in aqueous acetate buffer solutions using atomic force microscopy (AFM), providing valuable information concerning morphological data at the nanoscale level. The response of the three biosensing platforms developed, TvL/Au, TvL/DTSP/Au and TvL/MPTS/Au, is evaluated in the presence of hydroquinone (HQ), used as a phenolic enzymatic substrate. All systems exhibit a clear electrocatalytic activity and HQ can be amperometrically determined at -0.10 V versus Ag/AgCl. However, the performance of biosensors - evaluated in terms of sensitivity, detection limit, linear response range, reproducibility and stability - depends clearly on the enzyme immobilization strategy, which allows establishing its influence on the enzyme catalytic activity. © 2013 Published by Elsevier B.V.
Publisher version (URL)http://dx.doi.org/10.1016/j.talanta.2013.05.045
URIhttp://hdl.handle.net/10261/94633
DOI10.1016/j.talanta.2013.05.045
Identifiersdoi: 10.1016/j.talanta.2013.05.045
issn: 0039-9140
e-issn: 1873-3573
Appears in Collections:(ICMM) Artículos
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