Manganese oxide functionalized silk fibers for enzyme mimics application

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T1 - Manganese oxide functionalized silk fibers for enzyme mimics application

AU - Singh, Manish

AU - Dey, Estera S.

AU - Dicko, Cedric

PY - 2020

Y1 - 2020

N2 - 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.

AB - 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.

KW - Enzyme-mimic

KW - Catalase

KW - Oxidase

KW - Peroxidase

KW - Functionalized silk

KW - Potentiometric titration

KW - pK distribution

U2 - 10.1016/j.reactfunctpolym.2020.104565

DO - 10.1016/j.reactfunctpolym.2020.104565

M3 - Article

JO - Reactive and Functional Polymers

JF - Reactive and Functional Polymers

SN - 1873-166X

M1 - 104565

ER -