Manganese oxide functionalized silk fibers for enzyme mimics application

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Bibtex

@article{b9351495dcc14f259712d5f6761023c1,
title = "Manganese oxide functionalized silk fibers for enzyme mimics application",
abstract = "The inorganic metal or metal-oxide nanoparticles (NPs) that mimic enzymes are of great interest due to improved physical and chemical properties compared with native enzymes. Here, we report that manganese dioxide (MnO2)-Silk exhibit catalase, oxidase, and peroxidase-like activities. The MnO2-Silk hybrid fibers effectively decomposed hydrogen peroxide (H2O2) and oxidized the typical horseradish peroxidase substrates, such as o-phenylenediamine (OPD), and 3,3′,5,5′- tetramethylbenzidine (TMB) in the presence or absence of H2O2. The oxidative properties of MnO2-Silk fiber hybrid showed an enzyme-like behavior for the catalase-like activity, oxidase-like activity, and peroxidase-like activity. The operational stability of the MnO2-Silk fiber hybrid over ten cycles showed a constant residual activity of about 25–30{\%} after 2–3 cycles indicating that MnO2-Silk fiber hybrid could be used as a satisfactory oxidoreductase enzyme mimics. Potentiometric titration was used to determine the surface charges of the MnO2-Silk catalyst. Together, we identified the reactive species as Mn1−x4+Mnx3+O2−x(OH)x with a pK of approximately 5.2. Our results have implications on the understanding of the catalytic origin and interaction of metal oxides NP with various biomaterials.",
keywords = "Enzyme-mimic, Catalase, Oxidase, Peroxidase, Functionalized silk, Potentiometric titration, pK distribution",
author = "Manish Singh and Dey, {Estera S.} and Cedric Dicko",
year = "2020",
doi = "10.1016/j.reactfunctpolym.2020.104565",
language = "English",
journal = "Reactive and Functional Polymers",
issn = "1873-166X",
publisher = "Elsevier",

}