<p>Bisphenol A is a well-known endocrine-disrupting chemical that threatens human health due to its presence in aquatic environments. Conventional water treatment methods are inadequate for eliminating micropollutants like Bisphenol A. Therefore, new treatment strategies are necessary to confront this challenge. Enzymes such as laccase offer a promising solution. However, free enzymes have limitations, including non-reusability and low operational stability. To overcome these drawbacks, enzyme immobilization is used. In this study, laccase was immobilized using a novel porous support that contributes to pollutant removal. An amino-functionalized zinc-based metal–organic framework was utilized to immobilize crude laccase produced by <i>Trametes</i> sp. Laccase was immobilized with an activity recovery of 64% and improved stability. The immobilized biocatalyst eliminated 91.5% of Bisphenol A, with an initial concentration of 20&#xa0;ppm in 12&#xa0;h. The enzyme contributed to 61.5% of the removal through biodegradation, while the remaining 30% was due to physical adsorption by the metal–organic framework.</p> Graphical abstract <p></p>

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Immobilization of laccase using metal–organic frameworks for simultaneous biodegradation and adsorption of Bisphenol A

  • R. Ghassemi,
  • Z. Ghobadi Nejad,
  • S. Yaghmaei

摘要

Bisphenol A is a well-known endocrine-disrupting chemical that threatens human health due to its presence in aquatic environments. Conventional water treatment methods are inadequate for eliminating micropollutants like Bisphenol A. Therefore, new treatment strategies are necessary to confront this challenge. Enzymes such as laccase offer a promising solution. However, free enzymes have limitations, including non-reusability and low operational stability. To overcome these drawbacks, enzyme immobilization is used. In this study, laccase was immobilized using a novel porous support that contributes to pollutant removal. An amino-functionalized zinc-based metal–organic framework was utilized to immobilize crude laccase produced by Trametes sp. Laccase was immobilized with an activity recovery of 64% and improved stability. The immobilized biocatalyst eliminated 91.5% of Bisphenol A, with an initial concentration of 20 ppm in 12 h. The enzyme contributed to 61.5% of the removal through biodegradation, while the remaining 30% was due to physical adsorption by the metal–organic framework.

Graphical abstract