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用于双酚A生物转化的基于漆酶的催化微反应器。

Laccase-based catalytic microreactor for BPA biotransformation.

作者信息

Sosa-Hernández Juan Eduardo, Gutierrez Elsa M, Ochoa Sierra Jhosseph S, Aquines Osvaldo, Robledo-Padilla Felipe, Melchor-Martínez Elda M, Iqbal Hafiz M N, Parra-Salvídar Roberto

机构信息

Tecnologico de Monterrey, School of Engineering and Sciences, Monterrey, 64849, Mexico.

Tecnologico de Monterrey, Institute of Advanced Materials for Sustainable Manufacturing Monterrey, 64849, Mexico.

出版信息

Heliyon. 2024 Jan 11;10(2):e24483. doi: 10.1016/j.heliyon.2024.e24483. eCollection 2024 Jan 30.

Abstract

A laccase-based catalytic reactor was developed into a polydimethylsiloxane (PDMS) microfluidic device, allowing the degradation of different concentrations of the emergent pollutant, Bisphenol-A (BPA), at a rate similar to free enzyme. Among the immobilizing agents used, 1-Ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) was capable of immobilizing a more significant amount of the laccase enzyme in comparison to glutaraldehyde (GA), and the passive method (2989, 1537, and 1905 U/mL, respectively). The immobilized enzyme inside the microfluidic device could degrade 55 ppm of BPA at a reaction rate of 0.5309 U/mL*min with a contaminant initial concentration of 100 ppm at room temperature. In conclusion, the design of a microfluidic device and the immobilization of the laccase enzyme successfully allowed a high capacity of BPA degradation.

摘要

一种基于漆酶的催化反应器被开发成聚二甲基硅氧烷(PDMS)微流控装置,该装置能够以与游离酶相似的速率降解不同浓度的新兴污染物双酚A(BPA)。在所使用的固定剂中,与戊二醛(GA)相比,1-乙基-3-(3-二甲基氨基丙基)碳二亚胺(EDC)能够固定更多量的漆酶,以及被动方法(分别为2989、1537和1905 U/mL)。微流控装置内固定化的酶在室温下,对于初始浓度为100 ppm的污染物,能够以0.5309 U/mL·min的反应速率降解55 ppm的BPA。总之,微流控装置的设计和漆酶的固定化成功实现了对BPA的高降解能力。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c254/10827767/bb7906d818a6/ga1.jpg

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