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Manganese oxide functionalized silk fibers for enzyme mimics application

Singh, Manish (author)
Lund University,Lunds universitet,Tillämpad biokemi,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Pure and Applied Biochemistry,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
Dey, Estera S. (author)
Lund University,Lunds universitet,Tillämpad biokemi,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Pure and Applied Biochemistry,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
Dicko, Cedric (author)
Lund University,Lunds universitet,Tillämpad biokemi,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Pure and Applied Biochemistry,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
 (creator_code:org_t)
Elsevier BV, 2020
2020
English.
In: Reactive and Functional Polymers. - : Elsevier BV. - 1381-5148.
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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.

Subject headings

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

Keyword

Enzyme-mimic
Catalase
Oxidase
Peroxidase
Functionalized silk
Potentiometric titration
pK distribution

Publication and Content Type

art (subject category)
ref (subject category)

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Singh, Manish
Dey, Estera S.
Dicko, Cedric
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NATURAL SCIENCES
NATURAL SCIENCES
and Biological Scien ...
and Biochemistry and ...
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Reactive and Fun ...
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Lund University

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