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Self‐Assembled Complexes of Horseradish Peroxidase with Magnetic Nanoparticles Showing Enhanced Peroxidase Activity
Author(s) -
Corgié Stéphane C.,
Kahawong Patarawan,
Duan Xiaonan,
Bowser Daniel,
Edward Joseph B.,
Walker Larry P.,
Giannelis Emmanuel P.
Publication year - 2012
Publication title -
advanced functional materials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.069
H-Index - 322
eISSN - 1616-3028
pISSN - 1616-301X
DOI - 10.1002/adfm.201102398
Subject(s) - horseradish peroxidase , substrate (aquarium) , peroxidase , chemical engineering , materials science , nanoparticle , catalysis , magnetic nanoparticles , enzyme , nanomaterial based catalyst , nanotechnology , chemistry , organic chemistry , biology , ecology , engineering
Bio‐nanocatalysts (BNCs) consisting of horseradish peroxidase (HRP) self‐assembled with magnetic nanoparticles (MNPs) enhance enzymatic activity due to the faster turnover and lower inhibition of the enzyme. The size and magnetization of the MNPs affect the formation of the BNCs, and ultimately control the activity of the bound enzymes. Smaller MNPs form small clusters with a low affinity for the HRP. While the turnover for the bound fraction is drastically increased, there is no difference in the H 2 O 2 inhibitory concentration. Larger MNPs with a higher magnetization aggregate in larger clusters and have a higher affinity for the enzyme and a lower substrate inhibition. All of the BNCs are more active than the free enzyme or the MNPs (BNCs > HRP ≫ MNPs). Since the BNCs show surprising resilience in various reaction conditions, they may pave the way towards new hybrid biocatalysts with increased activities and unique catalytic properties for magnetosensitive enzymatic reactions.