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Journal of Nanoparticle Research

Erschienen in:

01.01.2015 | Research Paper

Catalytic activity of various pepsin reduced Au nanostructures towards reduction of nitroarenes and resazurin

Erschienen in: Journal of Nanoparticle Research | Ausgabe 1/2015

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Abstract

Pepsin, a digestive protease enzyme, could function as a reducing as well as stabilizing agent for the synthesis of Au nanostructures of various size and shape under different reaction conditions. The simple tuning of the pH of the reaction medium led to the formation of spherical Au nanoparticles, anisotropic Au nanostructures such as triangles, hexagons, etc., as well as ultra small fluorescent Au nanoclusters. The activity of the enzyme was significantly inhibited after its participation in the formation of Au nanoparticles due to conformational changes in the native structure of the enzyme which was studied by fluorescence, circular dichroism (CD), and infra red spectroscopy. However, the Au nanoparticle-enzyme composites served as excellent catalyst for the reduction of p-nitrophenol and resazurin, with the catalytic activity varying with size and shape of the nanoparticles. The presence of pepsin as the surface stabilizer played a crucial role in the activity of the Au nanoparticles as reduction catalysts, as the approach of the reacting molecules to the nanoparticle surface was actively controlled by the stabilizing enzyme.

Vorheriger Artikel High stability and reactivity of defective graphene-supported Fe n Pt13−n (n = 1, 2, and 3) nanoparticles for oxygen reduction reaction: a theoretical study

Nächster Artikel Synthesis of polystyrene@(silver–polypyrrole) core/shell nanocomposite microspheres and study on their antibacterial activities

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Titel: Catalytic activity of various pepsin reduced Au nanostructures towards reduction of nitroarenes and resazurin
Publikationsdatum: 01.01.2015
Erschienen in: Journal of Nanoparticle Research / Ausgabe 1/2015
Print ISSN: 1388-0764
Elektronische ISSN: 1572-896X
DOI: https://doi.org/10.1007/s11051-014-2835-y

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