Abstract
The novel inhibitory mechanism of thymol (2-isopropyl-5-methylphenol) on dopachrome formation by mushroom tyrosinase (EC 1.14.18.1) was identified. The UV-vis spectrum and oxygen consumption assays showed dopachrome formation using L-tyrosine as a substrate was suppressed by thymol. This inhibitory activity was reversed by the addition of a well-known radical scavenger, butylated hydroxyanisole (BHA). Further investigations using N-acetyl-L-tyrosine as a substrate with HPLC analysis suggested that thymol inhibits chemical redox reactions between dopaquinone and leukodopachrome instead of enzymatic reaction. This redox inhibitory activity of thymol was examined by using a model redox reaction with L-dihydroxyphenylalanine (L-DOPA) and p-benzoquinone. Thymol successfully inhibited oxidation of L-DOPA to dopaquinone, coupled with reduction of p-benzoquinone. Hence, the suppression of dopachrome formation by thymol is due to the inhibition of conversion of leukodopachrome to dopachrome. The antioxidant property of thymol is a key characteristic for the inhibitory mechanism of melanin synthesis.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
