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عنوان فارسی مقاله:
خصوصیات و بهینه سازی بیحرکتی کووالانسی اکسیداز گلوکز برای دستگاه های بیوالکتریک
عنوان انگلیسی مقاله:
Optimization and characterization of covalent immobilization of glucose oxidase for bioelectronic devices
سال انتشار : 2016
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مقدمه انگلیسی مقاله:
1. Introduction
In recent decades, there has been an increasing demand for small implantable biosensors or biofuel cells, causing less tissue damage or enabling patients to avoid surgery. Enzyme electrodes are one of the core components affecting the performance of these devices [1,2]. Electrode size should also be minimized for this purpose, which limits the space available to accommodate enzymes, thereby decreasing the power output or detection signals. The drawbacks associated with miniaturization can be overcome, if enzyme electrodes are fabricated to generate high electrical power or a large number of sensing signals per unit surface area of electrodes. To achieve this goal, electrode materials and immobilization methods should be improved to increase the enzyme loading on the electrode surface with strong binding [3]. Carbonnanotubes (CNTs) have recently attracted considerable attention in the field of bioelectronics, because they provide a large surface area for enzyme immobilization, better acceptable biocompatibility, chemical and electrochemical stability, and good electrical conductivity [4]. Many studies have shown that CNTs can be widely used as the modifying materials for the fabrication of biosensors and biofuel cells, in which the integration of CNTs into electrodes accelerated the electron transfer between electrode and enzymes [5–12]. CNTs were also used as effective electrical wiring/connectors between the electrodes and enzyme redox centers to overcome the kinetic barrier to electron transfer associated witha thickproteinlayer surrounding the redox center [13].Noncovalent (adsorption) and covalent immobilization on the surface of CNTs have been reported for various enzymes [10,14–16].Although physical adsorption methods are simple, and high enzyme loading can be achieved without the addition of reagents, immobilized enzymes can gradually be lost during use, because of weak bonding between the enzymes and the electrode surface [17]. Comparatively, covalentimmobilization provides more durable attachment, and thus immobilized enzymes survive over a longer operation time [17]. Therefore, CNT-electrodes covered with enzymes by covalent attachment are suitable for miniaturized implantable devices. However, covalent immobilization requires the chemical modification of CNTs or enzymes, and enzyme loading and activity vary depending on the reaction conditions. The coupling reaction mediated by 1-ethyl-3- (3-dimethylaminopropyl) carbodiimide (EDC) and N-hydroxysuccinimide (NHS) is one of the most attractive approaches for the covalent immobilization of enzymes onto the carboxyl-terminated surfaces in biosensors, because of its high conversion efficiency, mild reaction conditions, and excellent biocompatibility with a slight effect on the activity of target enzymes [18]. Many researchers immobilized enzymes on CNTs using EDC/NHS; however, extremely low enzyme loading was reported by this method. Although the immobilization efficiency is strongly affected by the pH, concentration of EDC and NHS, enzyme concentration, and reaction time [18], these factors for enzyme immobilization were not optimized. Therefore, there is significant room for the improvement in enzyme loading by immobilization using EDC/NHS. Recently, the EDC/NHS-mediated immobilization of biomolecules (amine or dopamine) on gold electrodes was reported, and the effects of EDC and NHS concentration, solution pH, reaction time, and biomolecule concentration on the immobilization efficiency were investigated by cyclic voltammetry [19,20].
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کلمات کلیدی:
Affinity Covalent Immobilization of Glucoamylase onto ρ ... link.springer.com/article/10.1007/s12010-010-9113-y by MSM Eldin - 2011 - Cited by 13 - Related articles Enzyme Immobilization and Characterization ... A novel affinity covalent immobilization technique of glucoamylase enzyme onto ρ-benzoquinone-activated ... Characterization of Surfaces Presenting Covalently Immobilized ... pubs.acs.org/doi/abs/10.1021/la101101a by Y Bai - 2010 - Cited by 10 - Related articles Apr 13, 2010 - Characterization of Surfaces Presenting Covalently Immobilized Oligopeptides Using Near-Edge X-ray Absorption Fine Structure Spectroscopy. Synthesis and characterization of covalently immobilized bis-crown ... xlink.rsc.org/?doi=B410410B&newsite=1 The synthesis of a novel covalently immobilized crown ether based potassium ionophore is presented. Apart from previously proposed methods for the ... Covalent immobilization of glucose oxidase on mesocellular silica ... https://www.researchgate.net/.../297615046_Covalent_immobilization_of_glucose_oxid... Glucose oxidase (GOx) immobilization onto mesoporous SBA-15 silica and two mesocellular foams (MCF) characterized by similar surface area and pore ... Peptides—Advances in Research and Application: 2012 Edition https://books.google.com/books?isbn=1464994986 2012 - Medical (2011 DEC 27) University of Wisconsin, Madison: Characterization of surfaces presenting covalently immobilized oligopeptides using near-edge X-ray ... Immobilization of Yarrowia lipolytica Lipase on Macroporous Resin ... https://www.hindawi.com/journals/bmri/2015/139179/ by J Sun - 2015 - Cited by 3 - Related articles Jun 21, 2015 - Cross-linkage method is to covalently bond enzymes together to ... on the immobilization and biochemical characteristics of Yarrowia lipolytica ...
