Electrical activity controlling system for a mediator-coexisting alcohol dehydrogenase-NAD conductive membrane

doi:10.1016/0022-0728(90)85100-J

Journal of Electroanalytical Chemistry and Interfacial Electrochemistry

Volume 277, Issues 1–2, 10 January 1990, Pages 179-187

https://doi.org/10.1016/0022-0728(90)85100-J Get rights and content

Abstract

A mediator-coexisting alcohol dehydrogenase-NAD conductive membrane was prepared by electro-chemical polymerization in a pyrrole solution containing alcohol dehydrogenase, NAD, and Meldola's blue. The polypyrrole membrane has enzyme activity as well as electroconductivity. NADH, produced enzymatically in the presence of ethyl alcohol, was oxidized with the aid of Meldola's blue in the membrane. The current of NADH oxidation was dependent on the alcohol concentration as well as the applied potential, i.e., the enzyme activity of the membrane was controlled electrically by the smooth and efficient electron transferring system, ethanol-enzyme-coenzyme-mediator, prepared in a polypyrrole matrix as a conductive interface.

References (26)

M. Aizawa et al.
Biochim. Biophys. Acta
(1976)
P.N. Bartlett et al.
J. Electroanal. Chem.
(1987)
L. Gorton et al.
J. Electroanal. Chem.
(1984)
L.G. Lee et al.
Appl. Biochem. Biotechnol.
(1987)
H. Jornvall et al.
J. Biol. Chem.
(1978)
M. Aizawa et al.
Proc. Int. Congress on Membranes and Membrane Process
(1987)
M. Aizawa et al.
O. Miyawaki et al.
Biotechnol. Bioeng.
(1984)
T. Ikeda et al.
Agric. Biol. Chem.
(1988)
N.S. Lewis et al.
Science
(1981)

F.A. Armstrong et al.

J. Am. Chem. Soc.

(1985)

A.F. Diaz et al.

J. Chem. Soc., Chem. Commun.

(1980)

G.B. Street et al.

Mol. Cryst. Liq. Cryst.

(1982)

Cited by (84)

NAD(P)-dependent glucose dehydrogenase: Applications for biosensors, bioelectrodes, and biofuel cells
2020, Bioelectrochemistry
Citation Excerpt :
Polyaminosaccharide chitosan chains can be considered as a convenient scaffold for covalent immobilisation of enzymes and redox cofactors, as well as for homogeneous dispersion of CNTs. Due to the restricted lifetime of both NAD+ and NADH, which are susceptible to decomposition in aqueous environments [124,125], co-immobilisation of NAD+ onto composite electrodes [126–129] or in electropolymerised layers [130] together with the enzyme and a mediator seems to be the preferred approach (see Table 2). In these systems, it is crucial that the mediated reaction is very fast, therefore, finding optimal mediators is an active area of research [131].
This review discusses the physical and chemical properties of nicotinamide redox cofactor dependent glucose dehydrogenase (NAD(P) dependent GDH) and its extensive application in biosensors and bio-fuel cells. GDHs from different organisms show diverse biochemical properties (e.g., activity and stability) and preferences towards cofactors, such as nicotinamide adenine dinucleotide (NAD⁺) and nicotinamide adenine dinucleotide phosphate (NADP⁺). The (NAD(P)⁺) play important roles in biological electron transfer, however, there are some difficulties related to their application in devices that originate from their chemical properties and labile binding to the GDH enzyme. This review discusses the electrode modifications aimed at immobilising NAD⁺ or NADP⁺ cofactors and GDH at electrodes. Binding of the enzyme was achieved by appropriate protein engineering techniques, including polymerisation, hydrophobisation or hydrophilisation processes. Various enzyme-modified electrodes applied in biosensors, enzymatic fuel cells, and biobatteries are compared. Importantly, GDH can operate alone or as part of an enzymatic cascade, which often improves the functional parameters of the biofuel cell or simply allows use of cheaper fuels. Overall, this review explores how NAD(P)-dependent GDH has recently demonstrated high potential for use in various systems to generate electricity from biological sources for applications in implantable biomedical devices, wireless sensors, and portable electronic devices.
Biomolecular immobilization on conducting polymers for biosensing applications
2007, Biomaterials
A detail study on different aspects of biomolecule immobilization techniques on conducting polymers (CP) for applications in biosensors is described. Comparative studies are conducted in between the different mode of biomolecule immobilization techniques, viz. physical, covalent and electrochemical immobilization onto the conducting polymer films for the fabrication of electrochemical biosensors for clinical, food and environmental monitoring applications. This review focuses on the current status of biomolecule immobilization techniques on CP and their applications in the development of amperometric biosensors.
Polymers in sensor applications
2004, Progress in Polymer Science (Oxford)
Because their chemical and physical properties may be tailored over a wide range of characteristics, the use of polymers is finding a permanent place in sophisticated electronic measuring devices such as sensors. During the last 5 years, polymers have gained tremendous recognition in the field of artificial sensor in the goal of mimicking natural sense organs. Better selectivity and rapid measurements have been achieved by replacing classical sensor materials with polymers involving nano technology and exploiting either the intrinsic or extrinsic functions of polymers. Semiconductors, semiconducting metal oxides, solid electrolytes, ionic membranes, and organic semiconductors have been the classical materials for sensor devices. The developing role of polymers as gas sensors, pH sensors, ion-selective sensors, humidity sensors, biosensor devices, etc., are reviewed and discussed in this paper. Both intrinsically conducting polymers and non-conducting polymers are used in sensor devices. Polymers used in sensor devices either participate in sensing mechanisms or immobilize the component responsible for sensing the analyte. Finally, current trends in sensor research and also challenges in future sensor research are discussed.
Electrocatalytic oxidation of NAD(P)H at mediator-modified electrodes
2002, Reviews in Molecular Biotechnology
Biomolecule immobilization on electrode surfaces by entrapment or attachment to electrochemically polymerized films. A review
1999, Biosensors and Bioelectronics
The concept and potentialities of electrochemical procedures of biomolecule immobilization based on electropolymerized films are described. The biomolecule entrapment in conventional electrogenerated polymers such as polypyrrole, polyaniline or polyphenol is compared with an electrochemical procedure involving the adsorption of amphiphilic monomers and biomolecules before the polymerization step. Examples of organic phase enzyme electrode and electrical wiring of immobilized enzymes are presented. Furthermore, the construction of controlled architectures based on spatially segregated multilayers, exhibiting complementary biological activities is described. Then, the use of functionalized polymers bearing functional groups for the covalent binding of biomolecules is reported. Moreover, the attachment of biomolecules to biotinylated polymers through affinity interactions based on avidin–biotin bridge is presented.
Determination of breath alcohol using a differential-type amperometric biosensor based on alcohol dehydrogenase
1999, Analytica Chimica Acta
A differential-type amperometric biosensor based on conventional thick-film technology has been developed for breath alcohol measurement. The amperometric breath alcohol biosensor utilizes the alcohol dehydrogenase (ADH) and nicotinamide adenine dinucleotide (NAD⁺) cofactor which produce reduced NADH as a product of the oxidation of alcohol. The biosensor was designed in a differential format consisting of a common Ag/AgCl reference electrode, an active working electrode containing the ADH, and the inactive working electrode containing only bovine serum albumin instead of the ADH. The differential signal between the active working electrode and the inactive working electrode minimized the interference from a large number of oxidizable species present in a person's breath. Prior to the amperometric measurement the biosensor was hydrated simply by dipping it into a phosphate buffer solution at pH 7.4. The NADH produced from the enzymatic reaction was oxidized at the working electrode biased at a potential of 470 mV vs. an on-board Ag/AgCl reference electrode. The biosensor can measure a person's breath alcohol over the concentration range 20–800 ppm routinely required in a test of drunken driving.

View all citing articles on Scopus

View full text

Electrical activity controlling system for a mediator-coexisting alcohol dehydrogenase-NAD conductive membrane

Abstract

Biochim. Biophys. Acta

J. Electroanal. Chem.

J. Electroanal. Chem.

Appl. Biochem. Biotechnol.

J. Biol. Chem.

Proc. Int. Congress on Membranes and Membrane Process

Biotechnol. Bioeng.

Agric. Biol. Chem.

Science

J. Am. Chem. Soc.

J. Chem. Soc., Chem. Commun.

Mol. Cryst. Liq. Cryst.