Journal
MICROCHIMICA ACTA
Volume 186, Issue 5, Pages -Publisher
SPRINGER WIEN
DOI: 10.1007/s00604-019-3451-4
Keywords
Enzyme mimetic; Oxidase-like activity; Tetramethylbenzidine; Inhibitory effect; o-Quinone; Kojic acid
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Funding
- National Natural Science Foundation of China [21675024, 21804021]
- Program for Innovative Leading Talents in Fujian Province [2016B016]
- Science and Technology Project of Fujian Province [2018 L3008]
- Natural Science Foundation of Fujian Province [2016 J01427, 2016 J06019]
- Startup Fund for scientific research, Fujian Medical University [2017XQ1014]
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It is found that catechol inhibits the oxidase-mimicking activity of chitosan-protected platinum nanoparticles (Chit-PtNPs) by competing with the substrate for the active site of the Ch-PtNPs. The inhibition mechanism of catechol is different from that of ascorbic acid in that it neither reacts with O-2(center dot-) nor reduces the oxidized 3,3,5,5-tetramethylbenzidine (TMB). Tyrosinase (TYRase) catalyzes the oxidation of catechol, thus restoring the activity of oxidase-mimicking Chit-PtNPs. By combining the Chit-PtNP, catechol, and TYRase interactions with the oxidation of TMB to form a yellow diamine (maximal absorbance at 450nm), a colorimetric analytical method was developed for TYRase determination and inhibitor screening. The assay works in the 0.5 to 2.5UmL(-1) TYRase activity range, and the limit of detection is 0.5UmL(-1). In our perception, this new assay represents a powerful approach for determination of TYRase activity in biological samples.
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