Highly selective colorimetric determination of catechol based on the aggregation-induced oxidase-mimic activity decrease of δ-MnO2.

Abstract

Multiple enzyme-like activities of manganese oxides (MnO2) have been reported and applied in catalysis, biosensors, and cancer therapy. Here, we report that catechol can be determined colorimetrically based on the 3,3′,5,5′-tetramethylbenzidine (TMB) oxidase-like activity of δ-MnO2. The detection was based on pre-incubation of catechol containing water samples with δ-MnO2, and then the residual TMB oxidase-like activity of reacted δ-MnO2 was linearly dependent on the catechol concentration in the range of 0.5 to 10 μM. This determination method was stable at pH 3.73–6.00 and was not affected by ion strength up to 200 μM. Common co-solutes in water bodies (50 μM) have negligible effects and excellent selectivity of catechol among various phenolic compounds (15 μM) was facilitated. Both reduction and aggregation of δ-MnO2 were observed during the incubation process with catechol, and aggregation-induced TMB oxidase–mimic activity decrease was the main factor for this colorimetric determination.