the peroxidase-like activity of butea monosperma mediated palladium nanoparticles for colorimetric detection of glucose

Nanostructured enzyme mimics are of great interest as promising alternatives to artificial enzymes for biomedical and catalytic applications. studying the chemical interactions between antioxidants and nano-enzymes may result in a better understanding of the capability of antioxidants and may help improve the function of artificial enzymes to better mimic natural enzymes. in this study, using palladium nanoparticles (pdnps) as peroxidase mimics to catalyze the oxidation of chromophoric substrates by h2o2, we developed a platform that acts as a biosensor for hydrogen peroxide and glucose and that can study the inhibitory effects of natural antioxidants on peroxidase mimics.the peroxidase-like activity of butea monosperma reduced palladium nanoparticles was assessed through using 3’,3’,5’,5’-tetramethyl benzidine(tmb) as a chromogen in the presence of h2o2. butea monosperma reduced palladium nanoparticles bm-pdnps catalytically oxidize tmb using h2o2, resulting in the production of a blue oxidation product. this product was measured and quantified using a uv-vis spectrophotometer at a wavelength (λmax) of 652 nm. the ph, temperature, and nanoparticle concentration are crucial factors in investigating the catalytic activity of bm-pdnps. the glucose oxidase enzyme catalyzes the production of gluconic acid, resulting in the release of h2o2 as a byproduct which can be subsequently be measured using bm-pdnps. under optimal conditions, the method exhibited a linear range of 1.5 µm to 1000 µm for glucose determination. the limit of detection (lod) calculated using the equation 3σ/m, was found to be 0.78 μm. the authenticity of the results obtained from bm-pdnps was confirmed through the use of uv-vis, fourier transform infrared spectroscopy (ftir) and transmission electron microscopy (tem).