Microfluidic devices and true‐color sensor as platform for glucose oxidase and laccase assays

Demirkol, Dilek Odaci; Dornbusch, Kay; Feller, K.‐H.; Tımur, Suna

doi:10.1002/elsc.201000068

Cited by 15 publications

(7 citation statements)

References 56 publications

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“…The length of the mixing channel and the flow rate in it determine the reaction time which has strong influence on signal strength, linear range and sensitivity of the measurement (Demirkol et al, 2011;Ohnishi et al, 2010;Songjaroen et al, 2009;Wu et al, 2007). For example, for absorbance measurements an optimum reaction time for the enzymatic reaction can be found that gives the strongest color development and hence the highest sensitivity (Wu et al, 2007).…”

Section: Mixingmentioning

confidence: 99%

Microfluidic enzymatic biosensing systems: A review

Mross

Pierrat

Zimmermann

et al. 2015

Biosensors and Bioelectronics

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Section: Mixingmentioning

confidence: 99%

Microfluidic enzymatic biosensing systems: A review

Mross

Pierrat

Zimmermann

et al. 2015

Biosensors and Bioelectronics

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“…Considering the industrial applicability, a low concentration of substrate may be a major restriction for the enzymatic reaction [27,28]. To test the feasibility of ArEH in the production of chiral epichlorohydrin and its potential for industrial application, the effect of the racemic epichlorohydrin concentration on the resolution was studied at various concentrations ranging from 25.6 to 384 mM ( Table 1).…”

Section: Effect Of the Substrate Concentration On The Reactionmentioning

confidence: 99%

Biosynthesis of (R)‐epichlorohydrin at high substrate concentration by kinetic resolution of racemic epichlorohydrin with a recombinant epoxide hydrolase

Jin

Liu

et al. 2013

Engineering in Life Sciences

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Research ArticleBiosynthesis of (R)-epichlorohydrin at high substrate concentration by kinetic resolution of racemic epichlorohydrin with a recombinant epoxide hydrolaseThe substrate concentration and yield were shown to be very low in the production of (R)-epichlorohydrin by hydrolysis of racemic epichlorohydrin using epoxide hydrolases in previous studies. In this work, we synthesized an epoxide hydrolase gene from Agrobacterium radiobacter and expressed it in Escherichia coli by the PCR assembly method. The recombinant A. radiobacter epoxide hydrolase (ArEH) was applied in the preparation of (R)-epichlorohydrin and, a yield of 42.7% with ≥99% enantiomeric excess (ee) from 25.6 mM racemic epichlorohydrin was obtained. However, the ee of (R)-epichlorohydrin was not able to reach 99% due to substrate and product inhibition when the substrate concentration was over 320 mM. Inhibition studies revealed that (S)-3-chloro-1,2-propanediol displayed noncompetitive inhibition in the conversion of (S)-epichlorohydrin but non-significant inhibition for (R)-epichlorohydrin. Moreover, ArEH was successfully applied in the preparation of (R)-epichlorohydrin at high substrate concentration by eliminating the substrate inhibition. The substrate concentration increased to 448 mM by intermittent feeding of the substrate and to 512 mM by using a two-phase reaction system, with a high yield (>27%) and ee (>98%) of (R)-epichlorohydrin. This is the first report of high-yield production of (R)-epichlorohydrin at high substrate concentration, laying the foundations for its application on the industrial scale.

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“…The integration of enzyme assays in microfluidic systems has been reported with the aim to quantify specific analytes in food and medical samples (Atalay et al 2009a;Laiwattanapaisal et al 2009;Vergauwe et al 2011), to screen and characterize enzyme inhibitors (Hadd et al 1997;Boer et al 2005) and to measure enzyme activity (Clark et al 2009;Demirkol et al 2011). With respect to the implementation of enzyme assays in microfluidic systems, differentiation is made between heterogeneous and homogeneous systems.…”

Section: Introductionmentioning

confidence: 98%

“…On the other hand, enzymatic assays are also executed on microfluidic platforms driven by pressure micropumps. For instance, Demirkol et al (2011) have successfully developed a simple method to determine the enzyme activities of glucose oxidase and laccase on microfluidic chip.…”

Section: Introductionmentioning

confidence: 99%

Sequential enzymatic quantification of two sugars in a single microchannel

Atalay

Vermeir

Vergauwe

et al. 2011

Microfluid Nanofluid

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This paper presents the implementation of a multiple analyte enzyme assay, based on the sequential injection of the different enzyme solutions, in an electrokinetic driven microfluidic chip. The assay methodology for the simultaneous quantification of D-glucose and D-fructose was reported in previous publications but here the real integration of both enzyme assays was achieved. When assays were executed separately, good reproducibility was observed with average CV values of 5.2% and 4.5% for the D-glucose and D-fructose assay, respectively. Next, the assays for the quantification of D-glucose and D-fructose were integrated simultaneously on chip, where each assay was executed consecutively in the same microreactor by applying a specific sequence of potentials at the reservoirs. This article proves the integration of a sequential based quantification approach in continuous microfluidic chips with electrokinetic actuation.

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Microfluidic devices and true‐color sensor as platform for glucose oxidase and laccase assays

Cited by 15 publications

References 56 publications

Microfluidic enzymatic biosensing systems: A review

Microfluidic enzymatic biosensing systems: A review

Biosynthesis of (R)‐epichlorohydrin at high substrate concentration by kinetic resolution of racemic epichlorohydrin with a recombinant epoxide hydrolase

Sequential enzymatic quantification of two sugars in a single microchannel

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