1. School of Chemical Engineering and Technology, State Key Laboratory of Chemical Engineering, Tianjin University, Tianjin 300350, China 2. The Co-Innovation Centre of Chemistry and Chemical Engineering of Tianjin, Tianjin 300350, China 3. Tianjin Key Laboratory of Membrane Science and Desalination Technology, Tianjin 300350, China
Recently, many efforts have been dedicated to creating enzyme-mimicking catalysts to replace natural enzymes in practical fields. Inspired by the pathological biomineralization behaviour of L-cystine, in this study, we constructed a laccase-like catalyst through the co-assembly of L-cystine with Cu ions. Structural analysis revealed that the formed catalytic Cu-cystine nanoleaves (Cu-Cys NLs) possess a Cu(I)-Cu(II) electron transfer system similar to that in natural laccase. Reaction kinetic studies demonstrated that the catalyst follows the typical Michaelis-Menten model. Compared with natural laccase, the Cu-Cys NLs exhibit superior stability during long-term incubation under extreme pH, high-temperature or high-salt conditions. Remarkably, the Cu-Cys NLs could be easily recovered and still maintained 76% of their activity after 8 cycles. Finally, this laccase mimic was employed to develop a colorimetric method for epinephrine detection, which achieved a wider linear range (9–455 μmol·L−1) and lower limit of detection (2.7 μmol·L−1). The Cu-Cys NLs also displayed excellent specificity and sensitivity towards epinephrine in a test based on urine samples.
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Q Tian, X Dou, L Huang, L Wang, D Meng, L Zhai, Y Shen, C You, Z Guan, X Liao. Characterization of a robust cold-adapted and thermostable laccase from Pycnoporus sp. SYBC-l10 with a strong ability for the degradation of tetracycline and oxytetracycline by laccase-mediated oxidation. Journal of Hazardous Materials, 2020, 382: 121084 https://doi.org/10.1016/j.jhazmat.2019.121084
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