Novel grafted electrochemical interface for covalent glucose oxidase immobilization using reactive pentafluorophenyl methacrylate
Author
Artigues Cladera, Margalida
Oh, Sejin
Abellà, Jordi (Abellà i Iglesias)
Borrós i Gómez, Salvador
Colominas Fuster, Sergi
Other authors
Universitat Ramon Llull. IQS
Publication date
2018-12-01ISSN
0927-7765
Abstract
One of the most important factors for the proper functioning of enzymatic electrochemical biosensors is the enzyme immobilization strategy. In this work, glucose oxidase was covalently immobilized using pentafluorophenyl methacrylate (PFM) by applying two different surface modification techniques (plasma polymerization and plasma-grafting). The grafted surface was specifically designed to covalently anchor enzyme molecules. It was observed using QCM-D measurements the PFM plasma-grafted surfaces were able to retain a higher number of active enzyme molecules than the PFM polymerized surfaces. An amperometric glucose biosensor using titanium dioxide nanotubes array (TiO2NTAs) modified by PFM plasma-grafted surface was prepared. The resulting biosensor exhibited a fast response and short analysis time (approximately eight minutes per sample). Moreover, this biosensor achieved high sensitivity (9.76 μA mM−1) with a linear range from 0.25 to 1.49 mM and a limit of detection (LOD) equal to 0.10 mM of glucose. In addition, the glucose content of 16 different food samples was successfully measured using the developed biosensor. The obtained results were compared with the respective HPLC value and a deviation smaller than 10% was obtained in all the cases. Therefore, the biosensor was able to overcome all possible interferences in the selected samples/matrices.
Document Type
Article
Document version
Accepted version
Language
English
Subject (CDU)
547 - Organic chemistry
Keywords
Electrochemical biosensor
Plasma modification
Hydroxyethyl methacrylate (HEMA)
QCM-D
Glucose oxidase
Surface engineering
Pages
9 p.
Publisher
Elsevier
Is part of
Colloids and Surfaces B: Biointerfaces
This item appears in the following Collection(s)
Rights
© Elsevier
Except where otherwise noted, this item's license is described as http://creativecommons.org/licenses/by-nc-nd/4.0/