Repetitive enzymatic determination of glucose with regeneration and recycling of coenzyme and enzymes

Roehrig, P.; Wolff, Charles‐Michel; Schwing, Jean-Paul

doi:10.1016/s0003-2670(00)85501-4

Cited by 22 publications

(8 citation statements)

References 12 publications

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“…Cyclic reactions involving amplification are often the method of choice for the enzymatic determination of small amounts of biologically important compounds whose quantitation would be otherwise difficult (1)(2)(3)(4)(5)(6)(7)(8). Although its use in analytical chemistry has been limited, there is a resurgence of interest in enzyme amplification as a result of the need for better and more sensitive biological sensors (9).…”

Section: Introductionmentioning

confidence: 99%

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Flow injection analysis of L-lactate with enzyme amplification and amperometric detection

Asouzu¹,

Nonidez²,

Ho³

1990

Anal. Chem.

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A flow injection analysis method for the determination of the lactate anion with enzyme amplification and amperometric detection is described. The system utilizes an oxygen electrode for measurement of changes in the oxygen concentration in the flow stream. Two enzymes, lactate oxidase and lactate dehydrogenase, were randomly coimmobilized on aminopropyl controlled-pore glass (AMP-CPG) and packed into a reactor. beta-NADH was used as a coenzyme for the regeneration of lactate from pyruvate. The experimental conditions for the determination of the lactate anion were studied for this system by the simplex and the univariant methods. The results obtained under these two conditions were compared. The simplex experimental condition yielded a calibration curve whose linear portion had a slope that was 1.2 times greater than that of the linear portion of the curve obtained under univariant conditions. The limit of detection under simplex condition was 1.19 x 10(-7) M vs 3.29 x 10(-7) M lactate under univariant conditions. The relative standard deviation obtained for this system at 6 x 10(-6) M lactate (n = 10) was about 2.5% under simplex conditions and 3.6% under univariant maximization conditions.

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Section: Introductionmentioning

confidence: 99%

“…Enzyme-mediated amplification has been used to analyze for a variety of substrtes (1)(2)(3)(4)(5)(6)(7)(8). The lactate oxidase/lactate dehydrogenase amplification cycle using /3-NADH//3-NAD"1" couple is by far the most reported scheme in the literature.…”

Section: Introductionmentioning

confidence: 99%

Flow injection analysis of L-lactate with enzyme amplification and amperometric detection

Asouzu¹,

Nonidez²,

Ho³

1990

Anal. Chem.

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“…Since 1980, a number of experiments have been reported in which NADH has been regenerated using electrochemical methods. , Direct electrochemical reduction of NAD + does not produce NADH; instead, a catalytically inactive dimer is formed . A common solution to this problem is to utilize two enzymes in the electrosynthesis; one enzyme transfers a reducing equivalent from an electrogenerated redox mediator to NAD + , while a second enzyme carries out the actual synthesis using the NADH produced in the first step. , The synthetic sequence is illustrated in Figure , where the first enzyme is lipoamide dehydrogenase (LiDH), the second enzyme is lactate dehydrogenase (LDH), and the redox mediator is methyl viologen (MV 2+ ) …”

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confidence: 99%

Cross-Linked LDH Crystals for Lactate Synthesis Coupled to Electroenzymatic Regeneration of NADH

et al. 1996

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Lactate dehydrogenase (LDH) was crystallized from concentrated ammonium sulfate solution and cross-linked with glutaraldehyde to afford long-lived enzymatically active cross-linked crystals (LDH-CLC). The crystals were employed in an electrolytic cell for lactate production from pyruvate, in which the cathode consisted of a carbon electrode containing a coating of lipoamide dehydrogenase (LiDH) immobilized with methyl viologen under a Nafion membrane. This cell was more effective than a similar cell containing LDH in soluble form. An even greater improvement in performance was achieved by chemically binding a viologen derivative to the LiDH and using an electrode based on this modified enzyme in a cell containing LDH-CLC. The activity of the LDH-CLC is much less sensitive to pH than that of the soluble enzyme.

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“…In this paper multidetection has been used to apply the basic kinetic principles to unsegmented flow systems, to obtain the conventional kinetic parameters, and to adapt and compare the conventional methods for kinetic determination of a species. The configuration suggested to perform this type 0003-2700/85/0357-1803Í01.50/0 of multidetection is quite simple, uses a single spectrophotometer as detector and is similar to the "closed loop" configurations described in the literature (19)(20)(21)(22)(23)(24)(25). However, there are two major differences: (a) The system does not remain constantly closed, but there is a solution draining for each sample once the physical equilibrium has been obtained, (b) There is no unit devoted to species regeneration.…”

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confidence: 99%

Multidetection in unsegmented flow systems with a single detector

Ríos¹,

Castro²,

Valcárcel³

1985

Anal. Chem.

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Repetitive enzymatic determination of glucose with regeneration and recycling of coenzyme and enzymes

Cited by 22 publications

References 12 publications

Flow injection analysis of L-lactate with enzyme amplification and amperometric detection

Flow injection analysis of L-lactate with enzyme amplification and amperometric detection

Cross-Linked LDH Crystals for Lactate Synthesis Coupled to Electroenzymatic Regeneration of NADH

Multidetection in unsegmented flow systems with a single detector

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