A Novel Glucose Sensor with a Glucose Oxidase Monolayer Immobilized by the Langmuir–Blodgett Technique

Tsuzuki, Hirohiko; Watanabe, Tadashi; Okawa, Yusuke; Yoshida, Shöichirö; Yano, Shigenobu; Koumoto, Kunihito; Komiyama, Makoto; Nihei, Yoshimasa

doi:10.1246/cl.1988.1265

Cited by 33 publications

(14 citation statements)

References 3 publications

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“…Behenic acid is an electrode on which the oxido-reduction of a reaction (99%) was provided by Sigma. The water was purified using product will occur have been developed in the last decade a Millipore system (Milli-RO and Milli-Q units) involving (1,(3)(4)(5)(6)(7)(8)(9)(10). The great advantage of the biosensors is their reverse osmosis, deionization, an active charcoal cartridge, short response times because of the thickness of the LB and filtration.…”

Section: Methodsmentioning

confidence: 99%

Mixed Langmuir Films of Glucose Oxidase and Behenic Acid: Structure and Dynamics

Dubreuil

Alexandre

Fiol

et al. 1996

Journal of Colloid and Interface Science

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Section: Methodsmentioning

confidence: 99%

Mixed Langmuir Films of Glucose Oxidase and Behenic Acid: Structure and Dynamics

Dubreuil

Alexandre

Fiol

et al. 1996

Journal of Colloid and Interface Science

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“…In most of our previous works (9)(10)(11) hydrogen peroxide generated by glucose oxidation was directly oxidized on a tin oxide electrode. The high overpotential for direct oxidation of hydrogen peroxide necessitated sensor operation at +800 to +900 mV vs Ag/AgCI, so that electroactive substances present as impurities in samples are liable to interfere with the assay.…”

Section: Methodsmentioning

confidence: 99%

“…Though a direct electron transfer is possible between an electrode and a peroxidase catalyzing the reduction of hydrogen peroxide (4)(5)(6)8), this is generally a slow process on common electrode materials. An appropriate electron donor can mediate the electron transfer between peroxidase and an electrode (3,7), and hence such a mediator is expected to improve the performance of a peroxidase-based hydrogen peroxide sensor. In recent papers we described fabrication of glucose sensors modified with a glucose oxidase (GOx) monolayer (9)(10)(11). Chemical immobilization of an enzyme as a monolayer gives 1 Present address: Department of Image Science and Engineering, Faculty of Engineering, Chiba University, Yayoi-cho, Chiba 260, Japan.…”

Section: Introductionmentioning

confidence: 99%

Enzyme monolayer- and bilayer-modified tin oxide electrodes for the determination of hydrogen peroxide and glucose

Tatsuma¹,

Okawa²,

Watanabe³

1989

Anal. Chem.

183

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An enzyme-based amperometrlc biosensor for hydrogen peroxide was developed, employing a horseradish peroxidase (HRP) monolayer covalently attached to a tin oxide electrode and a dissolved electron mediator. The sensor can determine hydrogen peroxide at levels down to 10~* M and can be applied to a flow system. Stability of the electrode, kinetics of the surface process, and the efficiencies of different mediators were studied. As an extension, glucose oxidase (GOx) was chemically bound to the HRP-modMed electrode. A GOx/HRP bilayer-modified electrode thus obtained exhibits much better performance in glucose detection limit, sensitivity, and response speed than previously reported GOx monolayer-modified electrodes.

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“…The Langmuir−Blodgett (LB) technique is one of the most powerful methods to prepare multilayered films, and many papers report on association of proteins to lipidic LB films. − However, such associations most often lack defined orientation of the protein, which results in a decrease of activity. Furthermore, the absence of strong interactions between the lipid matrix and the protein results in a rapid desorption of the latter.…”

Section: Introductionmentioning

confidence: 99%

New Functional Proteo-glycolipidic Molecular Assembly for Biocatalysis Analysis of an Immobilized Enzyme in a Biomimetic Nanostructure

et al. 2003

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A new organized biomimetic nanostructure embedding a monoclonal antibody in a lipidic matrix has been designed to sequester a hydrophilic enzyme in an oriented position and allowed to preserve the enzyme activity over a few months. The nanostructure was constituted of a glycolipid and a noninhibitory monoclonal IgG directed against the soluble form of acetylcholinesterase (AChE). A mixed monolayer (IgG-glycolipid) was obtained by spreading mixed IgG-glycolipid vesicles at the air/buffer interface. Several measurements (π-A isotherms, surface potential measurements, and compression-decompression cycles) allowed us to demonstrate the presence of IgG in the monolayer, as well as a reorientation of IgG molecules during the compression. After transfer on solid supports by the Langmuir-Blodgett technique, the presence of IgG in the mixed monolayer was characterized by ATR FTIR spectroscopy. Linking of the AChE on the IgG-glycolipid matrix was realized by immunoaffinity, and the enzyme was shown to retain its activity. The opportunity to detect a strong enzymatic activity, even after transfer at high surface pressures, suggested a preferential orientation of the antibody, favorable to retain the enzyme active at the surface of the nanostructure. The homogeneity of the transferred monolayer before and after immunoassociation, observed by Nomarski microscopy, did not display any structural modification. The enzyme kinetics was typical of the biocatalytic behavior of an immobilized enzyme, with a decrease of reaction rates due to the lower accessibility to the substrate at higher enzyme content. With the advantages of stability and favorable orientation of IgG, this new active matrix induces, in turn, a favorable orientation of the enzyme bound by immunoaffinity. The typical enzymatic behavior of the ternary nanostructure (glycolipid-IgG-AChE) demonstrates the usefulness of such a functional molecular assembly for biocatalysis study in a biomimetic situation.

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A Novel Glucose Sensor with a Glucose Oxidase Monolayer Immobilized by the Langmuir–Blodgett Technique

Abstract: A monomolecular layer of glucose oxidase (GOD) was immobilized on an SnO2 electrode via glutaraldehyde-bridged covalent bonding of GOD to the amino moieties of an octadecylamine Langmuir–Blodgett film. The performance of the electrode as an amperometric glucose sensor was investigated.

Cited by 33 publications

References 3 publications

Mixed Langmuir Films of Glucose Oxidase and Behenic Acid: Structure and Dynamics

Mixed Langmuir Films of Glucose Oxidase and Behenic Acid: Structure and Dynamics

Enzyme monolayer- and bilayer-modified tin oxide electrodes for the determination of hydrogen peroxide and glucose

New Functional Proteo-glycolipidic Molecular Assembly for Biocatalysis Analysis of an Immobilized Enzyme in a Biomimetic Nanostructure

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