Peroxidase Mimic Activities of Copper Selenide (CuSe) Nanoplates for Sensing H?O? and L-Cysteine.

Title Peroxidase Mimic Activities of Copper Selenide (CuSe) Nanoplates for Sensing H?O? and L-Cysteine.
Authors B. Maojuan; X. Chengcheng; H. Xuanye; L. Yanan; W. Jun
Journal J Nanosci Nanotechnol
DOI 10.1166/jnn.2020.17856
Abstract

Compared with natural enzymes, artificial mimic enzymes have been widely studied for their high stability and cost effectiveness. In this study, CuSe nanoplates as a simulated enzyme which does not contain precious metals, has peroxidase activity. CuSe nanoplates were prepared and characterized by powder X-ray diffraction (XRD), scanning electron microscopy (SEM), transmission electron microscopy (TEM) and X-ray energy dispersive spectrometer (EDS). Kinetic studies show that CuSe nanoplates exhibits a higher affinity for 3,3',5,5'-teramethylbenzidine (TMB) than horseradish peroxidase (HRP). The rapid colorimetric determination of H?O? and L-cysteine were developed based on the catalytic efficiency. The linear range of detection for H?O? is 5.0×10~8.0×10 M, and the detection limit is 2.9×10 M, while the relative standard error is less than 5%. In addition, L-cysteine was detected with a detection limit of 0.2×10 M. The good selectivity of the determination to H?O? and L-cysteine in aqueous solution was also achieved. CuSe nanoplates as a simulated enzyme for sensor applications would be used in environmental monitoring and biomedical analysis.

Citation B. Maojuan; X. Chengcheng; H. Xuanye; L. Yanan; W. Jun.Peroxidase Mimic Activities of Copper Selenide (CuSe) Nanoplates for Sensing H?O? and L-Cysteine.. J Nanosci Nanotechnol. 2020;20(9):53695375. doi:10.1166/jnn.2020.17856

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