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• W3145796379 startingPage "101109" @default.
• W3145796379 abstract "Cu-CuFe2O4 exhibited excellent activity as a peroxidase, which the affinity to H2O2 was significantly enhanced. However, the affinity to 3, 3’, 5, 5’- tetramethylbenzidine (TMB, another substrate) was weaker than Horseradish enzyme (HRP, a natural enzyme). At the present, Cu-CuFe2O4 was modified by an anionic surfactant (sodium dodecyl benzene sulfonate, SDBS) through a one-step method, which was named as SDBS-Cu-CuFe2O4. More negative zeta potential was found for SDBS-Cu-CuFe2O4, and the affinity to positive charged TMB was enhanced. The peroxidase-like activity and the peroxidase-like activity of per unit concentration were also improved. The catalytic efficiency was increased for TMB as the substrate. Effects on peroxidase-like activity of SDBS-Cu-CuFe2O4, such as zeta potential, redox ability, electron transfer and order of the addition of TMB and H2O2 in the system, were studied in detail. The peroxidase-like mechanism was proposed. SDBS-Cu-CuFe2O4 was used to rapidly detect H2O2 and dopamine (DA) with the smallest limit than reported." @default.
• W3145796379 created "2021-04-13" @default.
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• W3145796379 date "2021-06-01" @default.
• W3145796379 modified "2023-10-08" @default.
• W3145796379 title "Improvement of peroxidase-like activity and application for detection of H2O2 and dopamine for SDBS-Cu-CuFe2O4" @default.
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• W3145796379 doi "https://doi.org/10.1016/j.surfin.2021.101109" @default.
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