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      Electrochemical Affinity Biosensors Based on Disposable Screen-Printed Electrodes for Detection of Food Allergens

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          Abstract

          Food allergens are proteins from nuts and tree nuts, fish, shellfish, wheat, soy, eggs or milk which trigger severe adverse reactions in the human body, involving IgE-type antibodies. Sensitive detection of allergens in a large variety of food matrices has become increasingly important considering the emergence of functional foods and new food manufacturing technologies. For example, proteins such as casein from milk or lysozyme and ovalbumin from eggs are sometimes used as fining agents in the wine industry. Nonetheless, allergen detection in processed foods is a challenging endeavor, as allergen proteins are degraded during food processing steps involving heating or fermentation. Detection of food allergens was primarily achieved via Enzyme-Linked Immuno Assay (ELISA) or by chromatographic methods. With the advent of biosensors, electrochemical affinity-based biosensors such as those incorporating antibodies and aptamers as biorecognition elements were also reported in the literature. In this review paper, we highlight the success achieved in the design of electrochemical affinity biosensors based on disposable screen-printed electrodes towards detection of protein allergens. We will discuss the analytical figures of merit for various disposable screen-printed affinity sensors in relation to methodologies employed for immobilization of bioreceptors on transducer surface.

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          Most cited references110

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          High-affinity nucleic acid ligands for a protein were isolated by a procedure that depends on alternate cycles of ligand selection from pools of variant sequences and amplification of the bound species. Multiple rounds exponentially enrich the population for the highest affinity species that can be clonally isolated and characterized. In particular one eight-base region of an RNA that interacts with the T4 DNA polymerase was chosen and randomized. Two different sequences were selected by this procedure from the calculated pool of 65,536 species. One is the wild-type sequence found in the bacteriophage mRNA; one is varied from wild type at four positions. The binding constants of these two RNA's to T4 DNA polymerase are equivalent. These protocols with minimal modification can yield high-affinity ligands for any protein that binds nucleic acids as part of its function; high-affinity ligands could conceivably be developed for any target molecule.
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                Author and article information

                Contributors
                Role: Academic Editor
                Role: Academic Editor
                Journal
                Sensors (Basel)
                Sensors (Basel)
                sensors
                Sensors (Basel, Switzerland)
                MDPI
                1424-8220
                05 November 2016
                November 2016
                : 16
                : 11
                : 1863
                Affiliations
                [1 ]International Centre of Biodynamics, 1B Intrarea Portocalelor, sector 6, 060101 Bucharest, Romania; avasilescu@ 123456biodyn.ro
                [2 ]Technological Chemistry Department, Federal University of Maranhão, CCET/UFMA, Av. Portugueses, Cidade Universitária do Canga, 65080-040 São Luis, MA, Brazil; gilvanda.nunes@ 123456hotmail.com
                [3 ]Interdisciplinary Research Centre in Biomedical Materials (IRCBM) COMSATS Institute of Information Technology (CIIT), 54000 Lahore, Pakistan; akhtarhayat@ 123456ciitlahore.edu.pk (A.H.); usmanlatif@ 123456ciitlahore.edu.pk (U.L.)
                [4 ]BAE Laboratory, Université de Perpignan Via Domitia, 52 Avenue Paul Alduy, 66860 Perpignan, France
                Author notes
                [* ]Correspondence: jlmarty@ 123456univ-perp.fr ; Tel.: +33-468-66-1756
                Article
                sensors-16-01863
                10.3390/s16111863
                5134522
                27827963
                7796d4a3-0527-426f-8a51-be24a20a2581
                © 2016 by the authors; licensee MDPI, Basel, Switzerland.

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 21 September 2016
                : 31 October 2016
                Categories
                Review

                Biomedical engineering
                screen-printed electrode,allergen,biosensor,electrochemical detection,aptamer,antibody

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