Peroxidase activity was evaluated using ABTS-mediated colorimetric assays. A 96-well plate was prepared with 15 μl of OA nanozyme (2.27 × 10 7 particle per mL), 15 μl of H2O2 (final concentration of 100 μM), and 6 mM of ABTS in a 105 μl solution of sodium acetate-acetic acid buffer (70 mM final, pH 4.0). Concurrently, control groups were established by substituting H2O2 with deionized water and replacing the nanozyme with buffer. The catalytic oxidation of ABTS was assessed by monitoring the absorbance alterations of the oxidized ABTS form at λmax = 417 nm. Absorbance spectra were obtained over a wavelength range of 400 nm to 500 nm, with each group scanned thrice through a microplate reader. Steady-state kinetic characteristics were ascertained by measuring absorbance signals in kinetic mode utilizing Varian Cary 5G and Agilent Cary 5000 instruments. The reaction mixture comprised 700 μl of NaAc buffer, 100 μl of the OA nanozyme, 100 μl of the substrate (e.g., H2O2) located on a transparent cuvette, and varying concentrations of other substrate volumes as a 100 μl (e.g., ABTS). Absorbance endpoint peak signals were consistently recorded for up to 1 minute, respectively. Kinetic parameters were derived from the Michaelis-Menten equation, with Michaelis constant (Km) and maximum initial velocity (Vmax) obtained from Lineweaver-Burk plots and the corresponding Michaelis-Menten