Manganese oxide functionalized silk fibers for enzyme mimics application
(2020) In Reactive and Functional Polymers- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/b9351495-dcc1-4f25-9712-d5f6761023c1
- author
- Singh, Manish LU ; Dey, Estera S. LU and Dicko, Cedric LU
- organization
- publishing date
- 2020
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Enzyme-mimic, Catalase, Oxidase, Peroxidase, Functionalized silk, Potentiometric titration, pK distribution
- in
- Reactive and Functional Polymers
- article number
- 104565
- publisher
- Elsevier
- external identifiers
-
- scopus:85082393489
- ISSN
- 1381-5148
- DOI
- 10.1016/j.reactfunctpolym.2020.104565
- language
- English
- LU publication?
- yes
- id
- b9351495-dcc1-4f25-9712-d5f6761023c1
- date added to LUP
- 2020-03-13 16:53:24
- date last changed
- 2022-04-18 21:19:00
@article{b9351495-dcc1-4f25-9712-d5f6761023c1, 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.}}, author = {{Singh, Manish and Dey, Estera S. and Dicko, Cedric}}, issn = {{1381-5148}}, keywords = {{Enzyme-mimic; Catalase; Oxidase; Peroxidase; Functionalized silk; Potentiometric titration; pK distribution}}, language = {{eng}}, publisher = {{Elsevier}}, series = {{Reactive and Functional Polymers}}, title = {{Manganese oxide functionalized silk fibers for enzyme mimics application}}, url = {{http://dx.doi.org/10.1016/j.reactfunctpolym.2020.104565}}, doi = {{10.1016/j.reactfunctpolym.2020.104565}}, year = {{2020}}, }