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Halogenation of β-estradiol by a rationally designed mesoporous biocatalyst based on chloroperoxidase

Karina Salcedo
  • Instituto de Biotecnología, UNAM. Av. Universidad 2001, Chamilpa 62210 Cuernavaca, Mor. México
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Eduardo Torres-Ramírez
  • Posgrado en Ciencias Ambientales, Instituto de Ciencias, Benemérita Universidad Autónoma de Puebla. Edificio 103 G Ciudad Univesitaria 72570. Puebla, Pue. México
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Iliana Haces
  • Posgrado en Ciencias Ambientales, Instituto de Ciencias, Benemérita Universidad Autónoma de Puebla. Edificio 103 G Ciudad Univesitaria 72570. Puebla, Pue. México
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Marcela Ayala
  • Instituto de Biotecnología, UNAM. Av. Universidad 2001, Chamilpa 62210 Cuernavaca, Mor. México
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2015-04-29 | DOI: https://doi.org/10.1515/boca-2015-0001


Chloroperoxidase from Caldariomyces fumago was immobilized in Eupergit® C, a commercial mesoporous acrylic-based material. Due to low stability of the enzyme under neutral and basic pH, the usual covalent immobilization procedures cannot be applied to this enzyme. Several strategies were followed in order to achieve a stable interaction between the protein and the support. The support was efficiently functionalized with different reactive groups such as aromatic and aliphatic amines, glutaraldehyde, diazonium ions, and maleimide moieties; solvent-exposed amino acid residues in chloroperoxidase were identified or created through chemical modification, so that they were reactive under conditions where the enzyme is stable. Enzyme load and retained activity were monitored, obtaining biocatalysts with specific activity ranging from 200 to 25,000 U/g. The highest load and activity was obtained from the immobilization of a chemically-modified CPO preparation bearing a solvent-exposed free thiol group. This biocatalyst efficiently catalyzed the transformation of β-estradiol, an endocrine disruptor.

Keywords : Immobilization; chloroperoxidase; Eupergit® C; chemical modification; functionalization; stability


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About the article

Received: 2015-02-23

Accepted: 2015-04-05

Published Online: 2015-04-29

Citation Information: Biocatalysis, Volume 1, Issue 1, Pages 33–43, ISSN (Online) 2353-1746, DOI: https://doi.org/10.1515/boca-2015-0001.

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© 2015 Karina Salcedo et al.. This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License. BY-NC-ND 3.0

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