Final concentration of L-DOPA was maintained at 1 mM. The enzyme activity was measured kinetically at 1 min intervals for 30 min at 37 °C for the formation of dopachrome at 475 nm using a SpectraMax M5 microplate reader. The percent inhibition of tyrosinase activity was calculated as follows: % Inhibition ¼ ½ðA−BÞ=A 100
where A is the difference in absorption of the control sample between the samples with and without tyrosinase and B is the
difference in test sample between the samplewith andwithout tyrosinase [16].