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Paper microfluidic-based enzyme catalyzed double microreactor.

Ivonne M Ferrer1, Hector Valadez, Lissette Estala

  • 1Department of Chemistry and Biochemistry, California State University, Los Angeles, CA, USA.

Electrophoresis
|June 11, 2014
PubMed
Summary
This summary is machine-generated.

This study presents a simple, low-cost paper microfluidic device for enzyme-catalyzed assays. The microfluidic paper-based analytical device (μPAD) uses capillary action for a cascade reaction detecting lactic acid via fluorescence.

Keywords:
DiaphoraseDouble microreactorFluorescenceMicrofluidicsPaper-based chipResorufin

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Microfluidics

Background:

  • Enzyme-catalyzed assays are crucial for biochemical analysis.
  • Microfluidic paper-based analytical devices (μPADs) offer a low-cost and accessible platform for diagnostics.
  • Traditional methods often require complex enzyme immobilization or surface functionalization.

Purpose of the Study:

  • To develop a paper microfluidic device for enzyme-catalyzed assays.
  • To demonstrate a cascade reaction for detecting lactic acid using fluorescent detection.
  • To create a simplified assay that avoids enzyme immobilization.

Main Methods:

  • A microfluidic paper-based analytical device (μPAD) was fabricated by spotting lactate dehydrogenase (LDH) and diaphorase (DI) enzymes.
  • Samples containing lactic acid, resazurin, NAD(+), KCl, and BSA in MES buffer were spotted onto the μPAD.
  • Buffer flow through the device initiated a cascade reaction detected by fluorescence.

Main Results:

  • The μPAD facilitated a two-step enzymatic cascade reaction.
  • Lactate dehydrogenase (LDH) converted lactic acid to pyruvate and NADH.
  • Diaphorase (DI) then converted resazurin to fluorescent resorufin using NADH.

Conclusions:

  • The described paper microfluidic device offers a cost-effective and user-friendly approach for biochemical assays.
  • The assay effectively detects lactic acid through a fluorescent signal generated by a cascade reaction.
  • This method eliminates the need for enzyme immobilization, simplifying the assay procedure.