Metalloporphyrins immobilized in Fe sub(3)O sub(4)iO sub(2) mesoporous submicrospheres: Reusable biomimetic catalysts for hydrocarbon oxidation

We successfully immobilized metalloporphyrins (MeP) in mesoporous silica coating magnetite spheres. In this sense, we prepared two different classes of corehell supports, which comprise aligned (Fe sub(3)O sub(4)-AM-MeP, MeP = FeP or MnP) and non-aligned (Fe sub(3)O sub(4)-NM-MeP, MeP = FeP or MnP)...

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Bibliographic Details
Published in:Journal of colloid and interface science 2016-05, Vol.469, p.296-309
Main Authors: Barbosa, Isaltino A, Filho, Paulo Cde Sousa, Silva, Douglas Lda, Zanardi, Fabricio B, Zanatta, Lucas D, de Oliveira, Adilson JA, Serra, Osvaldo A, Iamamoto, Yassuko
Format: Article
Language:English
Subjects:
Catalysis
Catalysts
Diffraction
Magnetization
Oxidation
Reusable
Silicon dioxide
Transmission electron microscopy
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Summary:We successfully immobilized metalloporphyrins (MeP) in mesoporous silica coating magnetite spheres. In this sense, we prepared two different classes of corehell supports, which comprise aligned (Fe sub(3)O sub(4)-AM-MeP, MeP = FeP or MnP) and non-aligned (Fe sub(3)O sub(4)-NM-MeP, MeP = FeP or MnP) mesoporous magnetic structures. X-ray diffractometry and energy dispersive X-ray spectroscopy confirmed the mesoporous nature of the silica shell of the materials. Magnetization measurements, scanning and transmission electron microscopies (SEM/TEM), electrophoretic mobility ( zeta -potential), and infrared spectroscopy (FTIR) also confirm the composition and structure of the materials. The catalysts maintained their catalytic activity during nine reaction cycles toward hydrocarbon oxidation processes without detectable catalyst leaching. The catalysis results revealed a biomimetic pattern of cytochrome P450-type enzymes, thus confirming that the prepared materials are can effectively mimic the activity of such groups.
ISSN:0021-9797
DOI:10.1016/j.jcis.2016.01.059