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Laccase-based catalytic microreactor for BPA biotransformation.
Juan Eduardo Sosa-Hernández1,2, Elsa M Gutierrez3, Jhosseph S Ochoa Sierra4
1Tecnologico de Monterrey, School of Engineering and Sciences, Monterrey, 64849, Mexico.
Heliyon
|February 1, 2024
Summary
This study developed a microfluidic device using immobilized laccase enzyme for Bisphenol-A (BPA) degradation. The system efficiently removes BPA, demonstrating a promising method for pollutant remediation.
Area of Science:
- Environmental Science
- Biotechnology
- Chemical Engineering
Background:
- Emerging pollutants like Bisphenol-A (BPA) pose significant environmental risks.
- Enzyme-based degradation offers a sustainable approach to pollutant removal.
- Microfluidic devices provide controlled environments for catalytic processes.
Purpose of the Study:
- To develop a polydimethylsiloxane (PDMS) microfluidic device for laccase enzyme immobilization.
- To evaluate the degradation efficiency of immobilized laccase on Bisphenol-A (BPA).
- To compare different immobilization agents for optimal enzyme loading.
Main Methods:
- Laccase enzyme was immobilized onto a PDMS microfluidic chip using 1-Ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) and glutaraldehyde (GA).
- The catalytic activity of immobilized laccase was assessed by measuring the degradation rate of varying BPA concentrations.
- Reaction kinetics were analyzed at room temperature to determine degradation efficiency.
Main Results:
- EDC proved more effective than GA for immobilizing higher amounts of laccase enzyme.
- The microfluidic reactor successfully degraded 55 ppm of BPA from an initial concentration of 100 ppm.
- The immobilized enzyme achieved a degradation rate of 0.5309 U/mL*min, comparable to free enzyme activity.
Conclusions:
- A novel microfluidic reactor design integrating immobilized laccase was successfully developed.
- The system demonstrates high capacity and efficiency for Bisphenol-A (BPA) degradation.
- This approach offers a viable solution for the environmental remediation of endocrine-disrupting chemicals.

