Metalloporphyrins immobilized in Fe3O4@SiO2 mesoporous submicrospheres: Reusable biomimetic catalysts for hydrocarbon oxidation

JOURNAL OF COLLOID AND INTERFACE SCIENCE

卷:469

Article

Barbosa, Isaltino A.¹  de Sousa Filho, Paulo C.¹  da Silva, Douglas L.¹  Zanardi, Fabricio B.¹  Zanatta, Lucas D.¹  de Oliveira, Adilson J. A.²  Serra, Osvaldo A.¹  Iamamoto, Yassuko¹ 

[1] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Chem, Bioinorgan Chem & Rare Earth Labs, Ave Bandeirantes 3900, BR-14040901 Ribeirao Preto, SP, Brazil

[2] Univ Fed Sao Carlos, Dept Phys, Ave Trabalhador Sao Carlense,400 Pq Arnold Schimi, BR-13566590 Sao Carlos, SP, Brazil

关键词: Mesoporous structures;    Core@shell structures;    Magnetite particles;    Porphyrins;    Biomimetic catalysis;   

DOI  :  10.1016/j.jcis.2016.01.059

来源: Elsevier

【 摘 要 】

We successfully immobilized metalloporphyrins (MeP) in mesoporous silica coating magnetite spheres. In this sense, we prepared two different classes of core@shell supports, which comprise aligned (Fe3O4-AM-MeP, MeP = FeP or MnP) and non-aligned (Fe3O4-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. (C) 2016 Elsevier Inc. All rights reserved.

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