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Kinetics of Ergothioneine Inhibition of Mushroom Tyrosinase

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Abstract

The native amino acid ergothioneine, a thiourea derivative of histidine, inhibits mushroom tyrosinase activity in a dose-dependent manner, with an IC50 value of 1.025 mg/ml (4.47 mM). By contrast, histidine exhibited no inhibitory effect on mushroom tyrosinase activity. We characterized ergothioneine as a noncompetitive tyrosinase inhibitor using a Lineweaver–Burk plot of experimental kinetic data. The IC50 value for ergothioneine scavenging of 2,2-diphenyl-1-picrylhydrazyl was 6.110 ± 0.305 mg/ml, much higher than the IC50 for inhibition of tyrosinase activity which indicating ergothioneine on tyrosinase shows a weak correlation to its antioxidative activity. The results demonstrated that ergothioneine has a potent inhibition effect on tyrosinase enzyme activity, resulting from the presence of the sulfur substituted imidazole ring in ergothioneine.

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Acknowledgments

The authors thank the National Science Council, Taiwan, ROC for financial support (NSC99-2622-B-241-003-CC3).

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Correspondence to Chin-Feng Chan.

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Liao, W.C., Wu, W.H., Tsai, PC. et al. Kinetics of Ergothioneine Inhibition of Mushroom Tyrosinase. Appl Biochem Biotechnol 166, 259–267 (2012). https://doi.org/10.1007/s12010-011-9421-x

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  • DOI: https://doi.org/10.1007/s12010-011-9421-x

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