An enzyme electrode forl-lactate with a chemically-amplified response

https://doi.org/10.1016/S0003-2670(00)82947-5Get rights and content

Abstract

An enzyme electrode with a chemically-amplified response forl-lactate is constructed from an oxygen electrode and a layer containing immobilized lactate oxidase, to oxidizel-lactate, and lactate dehydrogenase, to regenerate thel-lactate. Regeneration enables oxygen to be consumed beyond the stoichiometric limitation, which results in an electrode response amplified 2–250 times according to the variation in the layer properties such as the Vmax and Km values of the immobilized enzymes and the thickness of the layer. The detection limit is as low as 5 × 10−9 M. An equation is derived to relate the rate of oxygen consumption in the layer to the experimental parameters; the equation successfully explains the experimental results.

Reference (41)

  • LowryO.H. et al.

    J. Biol. Chem.

    (1961)
  • KarubeI. et al.

    Anal. Chim. Acta

    (1980)
  • MatsunagaT. et al.

    Anal. Chim. Acta

    (1981)
  • MasciniM. et al.

    Anal. Chim. Acta

    (1984)
  • YaoT. et al.

    Anal. Chim. Acta

    (1982)
  • KoyamaM. et al.

    Anal. Chim. Acta

    (1980)
  • ZeweV. et al.

    J. Biol. Chem.

    (1962)
  • YaoT.

    Anal. Chim. Acta

    (1983)
  • BlaedelW.J. et al.

    Anal. Chem.

    (1978)
  • BergmeyerH.U.
  • LoworyO.H.

    Acc. Chem. Res.

    (1973)
  • GuilbaultG.G.
  • CarrP.W. et al.
  • DavisP. et al.

    Biochim. Biophys. Acta

    (1974)
  • BlaedelW.J. et al.

    Anal. Chem.

    (1976)
  • BlaedelW.J. et al.

    Anal. Chim. Acta

    (1980)
  • MizutaniF. et al.

    Chem. Lett.

    (1984)
  • MatsunagaT. et al.

    Eur. J. Appl. Microbiol. Biotechnol.

    (1982)
  • MizutaniF. et al.

    Anal. Chem.

    (1983)
  • MasciniM. et al.
  • Cited by (97)

    • Electrochemistry in bicontinuous microemulsions based on control of dynamic solution structures on electrode surfaces

      2016, Current Opinion in Colloid and Interface Science
      Citation Excerpt :

      This selectivity enables us to construct a current amplification system solely with the F-nanocarbon film electrode in combination with a ferrocene mediator and Fe2 + as a reductant, as outlined in Fig. 8(a)[39•]. Current amplification systems for electron transfer mediators have been widely studied using an enzyme-modified electrode to improve the sensitivity and detection limit of various biomolecules [44]. If a current amplification system is created by redox cycling with an F-nanocarbon film electrode, the system can be used for bioelectroanalysis with a lower concentration and a high S/N ratio because the electrochemical inactivity of the F-nanocarbon film suppresses the direct oxidation of Fe2 + ions at the fluorinated surface.

    • Fluorinated Nanocarbon Film Electrode Capable of Signal Amplification for Lipopolysaccharide Detection

      2016, Electrochimica Acta
      Citation Excerpt :

      We expect this selectivity to enable us to construct a current amplification system in combination with a relatively hydrophobic and outer-sphere ferrocene mediator and hydrophilic and inner-sphere Fe2+/3+ as a reductant. Current amplification systems for electron transfer mediators have been widely studied by using an enzyme-modified electrode to improve the sensitivity and detection limit of various biomolecules [20,21]. If we achieve a current amplification system by redox cycling with an F-nanocarbon film electrode as shown Fig. 1(a), we can expect to use this system for bioelectroanalysis with a lower concentration and a high S/N ratio because the electrochemical inactivity of the F-nanocarbon film suppresses the direct oxidation of Fe2+ ions at a fluorinated surface.

    • Mathematical model and numerical simulation of inhibition based biosensor for the detection of Hg(II)

      2015, Sensors and Actuators, B: Chemical
      Citation Excerpt :

      It was demonstrated that after exposure the glucose biosensor (without any additional reagents) to the high concentration equal to 1 ppm of methyl mercury the response of glucose remained constant, whereas the combination of very low concentration of invertase enzyme and 10 min of incubation time allows the detection of methyl mercury at very low concentration (ppb level) [17]. The mathematical models are a useful tool for the kinetic and geometric analysis of biosensors [18]; Models are developed to simulate enzymatic sensors [19–27] and different configurations composed of mono or multi-layer juxtaposed are investigated [28–31]. Several mathematical models have been developed to describe the amperometric response of glucose sensor [32–36].

    • Conductometric biosensors

      2014, Biological Identification: DNA Amplification and Sequencing, Optical Sensing, Lab-On-Chip and Portable Systems
    View all citing articles on Scopus
    View full text