Premium
Hierarchical Hybrid Peroxidase Catalysts for Remediation of Phenol Wastewater
Author(s) -
Duan Xiaonan,
Corgié Stéphane C.,
Aneshansley Daniel J.,
Wang Peng,
Walker Larry P.,
Giannelis Emmanuel P.
Publication year - 2014
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201300808
Subject(s) - phenol , horseradish peroxidase , catalysis , chemistry , peroxidase , magnetic nanoparticles , radical , reusability , phenols , substrate (aquarium) , chemical engineering , nanoparticle , immobilized enzyme , combinatorial chemistry , organic chemistry , enzyme , programming language , oceanography , software , computer science , engineering , geology
We report a new family of hierarchical hybrid catalysts comprised of horseradish peroxidase (HRP)–magnetic nanoparticles for advanced oxidation processes and demonstrate their utility in the removal of phenol from water. The immobilized HRP catalyzes the oxidation of phenols in the presence of H 2 O 2 , producing free radicals. The phenoxy radicals react with each other in a non‐enzymatic process to form polymers, which can be removed by precipitation with salts or condensation. The hybrid peroxidase catalysts exhibit three times higher activity than free HRP and are able to remove three times more phenol from water compared to free HRP under similar conditions. In addition, the hybrid catalysts reduce substrate inhibition and limit inactivation from reaction products, which are common problems with free or conventionally immobilized enzymes. Reusability is improved when the HRP–magnetic nanoparticle hybrids are supported on micron‐scale magnetic particles, and can be retained with a specially designed magnetically driven reactor. The performance of the hybrid catalysts makes them attractive for several industrial and environmental applications and their development might pave the way for practical applications by eliminating most of the limitations that have prevented the use of free or conventionally immobilized enzymes.