Applied Biochemistry and Biotechnology

, Volume 166, Issue 2, pp 259–267 | Cite as

Kinetics of Ergothioneine Inhibition of Mushroom Tyrosinase

  • Wayne C. Liao
  • Wen Hong Wu
  • Pei-Chuan Tsai
  • Hui-Feng Wang
  • Yi-Hsin Liu
  • Chin-Feng Chan
Article

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.

Keywords

Ergothioneine Histidine Tyrosinase DPPH 

Notes

Acknowledgments

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

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Copyright information

© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  • Wayne C. Liao
    • 1
  • Wen Hong Wu
    • 2
  • Pei-Chuan Tsai
    • 3
  • Hui-Feng Wang
    • 3
  • Yi-Hsin Liu
    • 3
  • Chin-Feng Chan
    • 3
  1. 1.Department of NursingChang Gung Institution of TechnologyChia-YiTaiwan
  2. 2.Plastic and Reconstructive Cosmetic Surgery CenterKuang Tien General HospitalTaichungTaiwan
  3. 3.Department of Applied CosmetologyHungkuang UniversityTaichungTaiwan

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