Tyrosinase Inhibition Kinetics of Anisic Acid

Abstract

Abstract Anisic acid (p-methoxybenzoic acid) was characterized as a tyrosinase inhibitor from aniseed, a common food spice. It inhibited the oxidation of l-3,4-dihydroxyphenylalanine (ʟ- DOPA) catalyzed by tyrosinase with an IC50 of 0.60 mᴍ. The inhibition of tyrosinase by anisic acid is a reversible reaction with residual enzyme activity. This phenolic acid was found to be a classical noncompetitive inhibitor and the inhibition constant KI was obtained as 0.603 mᴍ. Anisic acid also inhibited the hydroxylation of ʟ-tyrosine catalyzed by tyrosinase. The lag phase caused by the monophenolase activity was lengthened and the steady-state activity of the enzyme was decreased by anisic acid.