Elimination of electrooxidizable interferant-produced currents in amperometric biosensors

Maidan, Ruben; Heller, Adam

doi:10.1021/ac00047a003

Cited by 122 publications

(56 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The enzyme-loaded microcapsule arrays function as enzymatic bioreactors in both aqueous solution and organic solvents. 14 Immobilized enzymes are used in bioreactors and biosensors (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20). Current methods for immobilizing enzymes include adsorption or covalent attachment to a support (2)(3)(4), microencapsulation (5,6), and entrapment within a membrane/film (7,8,(11)(12)(13)(14)(15)(16)(17)(18)(19)(20) or gel (9 The synthetic methods developed are related to our work on polymeric microtubules (21)(22)(23)(24).…”

Section: Abstract (Maximum 200 Words)mentioning

confidence: 99%

Synthesis of polymeric microcapsule arrays and their use for enzyme immobilization

Parthasarathy

Martin

1994

Nature

328

198

View full text Add to dashboard Cite

Section: Abstract (Maximum 200 Words)mentioning

confidence: 99%

Synthesis of polymeric microcapsule arrays and their use for enzyme immobilization

Parthasarathy

Martin

1994

Nature

328

198

View full text Add to dashboard Cite

“…The biosensors should be operated at low electrode potential to circumvent the possible interference caused by oxidizable compounds such as ascorbic acid and uric acid. 12) From this viewpoint, Fc-CH 2 OH is considered to be the most suitable electron mediator for practical use for the determination of glucose or lactate.…”

Section: Resultsmentioning

confidence: 99%

Glucose and Lactate Biosensors Prepared by a Layer-by-Layer Deposition of Concanavalin A and Mannose-Labeled Enzymes: Electrochemical Response in the Presence of Electron Mediators.

Kobayashi

Hoshi

Anzai

2001

CHEMICAL & PHARMACEUTICAL BULLETIN

View full text Add to dashboard Cite

Enzyme biosensors have been widely studied because of their usefulness in bioanalytical science and technology. 1,2) In this context, we have developed high-performance glucose and lactate sensors using enzyme multilayer films which were prepared by a layer-by-layer deposition of monomolecular layers of avidin and biotin-labeled glucose oxidase (GOx) and lactate oxidase (LOx). [3][4][5] The output current of the multilayer film-modified biosensors can be controlled precisely by regulating the number of enzyme layers in the multilayer films; the size of the response current is proportional to the number of enzyme layers. [3][4][5] It was also possible to eliminate ascorbate interference by immobilizing ascorbate oxidase simultaneously in the GOx and LOx multilayer films.6) Thus, the enzyme multilayer films prepared by taking advantage of a strong affinity between avidin and biotin were quite useful for improving performance characteristics of enzyme biosensors.We recently reported another protocol to prepare enzyme multilayer films by means of the biological interaction between concanavalin A (Con A) and mannose. 7,8) Con A is a lectin protein (molecular weight; ca. 104000) and is known to contain four identical binding sites to a-D-mannose. 9) Con A and mannose-labeled GOx or LOx were deposited alternately on the surface of a platinum (Pt) electrode by immersing the electrode in the solutions of Con A and enzymes alternately, to fabricate the multilayer film-modified enzyme sensors. After this simple treatment, the enzymes were built into the multilayer films composed of monomolecular layers of Con A and enzymes on the electrode surface through the biological affinity between Con A and mannose. The enzyme/Con A multilayer-modified electrodes thus prepared could be used to determine glucose and lactate, where the electric current was originating from the electrochemical oxidation of hydrogen peroxide generated through the enzyme reactions (Eqs. 1, 2).In the present paper, as an alternative protocol for the operation of the enzyme sensors, a cyclic voltammetric response of the sensors is evaluated in the presence of ferrocene derivatives as electron mediator.Experimental GOx (EC 1.1.3.4, from Aspergillus niger, Sigma, St. Louis, U.S.A.), LOx (EC 1.1.3.2, from Pediococcus species, Boehringer Mannheim, Germany), and Con A (from Jack bean, Vector Lab., U.S.A.) were used as received. a-D-Mannopyranosylphenylisothiocyanate (MPITC) was purchased from Sigma Co. (St. Louis, U.S.A.). All other reagents were of the highest grade available and were used without further purification.Preparation of Mannose-Labeled Enzyme Mannose-labeled GOx and LOx were prepared as follows: 1 mg enzyme and 0.5 mg MPITC were dissolved in 0.1 M NaHCO 3 solution (0.5 ml), and the solution was stirred for 2 h at ca. 20°C. The unreacted MPITC was removed from the reaction mixture by centrifugal filtration. Several residues of mannose were introduced on the surface of the enzyme.Preparation of Enzyme Multilayer-Modified Electrode A Pt disk electrode...

show abstract

“…17 Ascorbic acid is available in blood at concentrations of ∼50 µM. 31,32 Figure 3 shows the current-time curves of Au/cyt c/PL:(XOD, AOD) observed at 0.15 V for the O2 -radical generated on the addition of xanthine in the presence and absence of 50 µM L-ascorbic acid. In the presence of Lascorbic acid, O2 -radical will be quenched by a reductive reaction (Eq.…”

Section: Amperometric Measurement Of Superoxide Radical and Sodmentioning

confidence: 99%

Amperometric Detection of Superoxide Dismutase at Cytochrome c-Immobilized Electrodes: Xanthine Oxidase and Ascorbate Oxidase Incorporated Biopolymer Membrane for in-vivo Analysis

Gobi

Mizutani

2001

ANAL. SCI.

View full text Add to dashboard Cite

Superoxide radical is highly reactive and short-lived and is formed in all aerobic cells. The superoxide radical generated during the "respiratory burst" of phagocytic cells plays an important role in the destruction of microorganisms invading into our body. But it may be involved in oxidative damage to tissues and organisms if it exceeds the level at which the systems are able to provide defence. The ubiquitous presence of SOD enzyme throughout the evolutionary chain emphasizes the importance of superoxide radical in cell function and survival. SOD plays a major protective role in living cells and has been widely used as a pharmacological tool in the study of pathophysiological mechanisms. 1-6 Detection of superoxide and SOD has been intensively pursued by spectrophotometric and electrochemical methods. [7][8][9][10][11][12][13][14][15][16] Electrochemical sensors are of great interest due to their advantages, which include microfabrication and in-vivo and in-vitro applications. 17,18 The hemoprotein, cytochrome c (cyt c), undergoes facile reductive reaction with superoxide. Electrochemical biosensors for superoxide with cyt c as the sensing element were constructed employing a suitable electron-transfer promoter.11-14 SOD is a selective scavenger of superoxide, and the best way for the detection of SOD thus could be the estimation of superoxide. Superoxide undergoes spontaneous disproportionation to produce H2O2, an electroactive species. Thus, the electrical response of the superoxide sensor system for interfering compounds is a very important limitation in its application. We recently reported a selective detection of superoxide and SOD at cyt c/alkanethiol electrodes, where the response due to interferents was suppressed by the use of a mixed-monolayer of alkanethiols for anchoring cyt c; but the presence of L-ascorbic acid, a potential scavenger of superoxide existing ubiquitously in our body, was detrimental to the detection of superoxide and SOD. 19 The detection of superoxide and consequently SOD in the presence of L-ascorbic acid was established using XOD/cyt c-bilayer electrodes, where the poly-L-lysine: polystyrenesulfonate complex membrane employed for the immobilization of XOD restricted the permeation of L-ascorbic acid across the membrane and consequently suppressed the scavenging of the superoxide produced at the membrane-bound XOD by Lascorbic acid. 20 The XOD/cyt c-bilayer electrodes could detect SOD in the presence of L-ascorbic acid; however, the sensitivity of XOD/cyt c-bilayer electrodes for SOD was rather low (detection limit, 0.2 µg ml -1 ) relative to that of cyt c-monolayer electrodes (detection limit, 3 ng ml -1 ); 19,20 the permeation of SOD across the polyion complex membrane confining XOD was suppressed in the case of the bilayer electrodes, which resulted into a low sensitivity for the detection of SOD. In the present investigation, the cyt c-immobilized monolayer electrodes were prepared by covalently-immobilizing cyt c on mixed-monolayers of 3-mercaptopropionic acid (MPA) with t...

show abstract

Elimination of electrooxidizable interferant-produced currents in amperometric biosensors

Cited by 122 publications

References 30 publications

Synthesis of polymeric microcapsule arrays and their use for enzyme immobilization

Synthesis of polymeric microcapsule arrays and their use for enzyme immobilization

Glucose and Lactate Biosensors Prepared by a Layer-by-Layer Deposition of Concanavalin A and Mannose-Labeled Enzymes: Electrochemical Response in the Presence of Electron Mediators.

Amperometric Detection of Superoxide Dismutase at Cytochrome c-Immobilized Electrodes: Xanthine Oxidase and Ascorbate Oxidase Incorporated Biopolymer Membrane for in-vivo Analysis

Contact Info

Product

Resources

About