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 (L-DOPA) catalyzed by tyrosinase with an IC 50 of 0.60 mM. 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 K I was obtained as 0.603 mM. Anisic acid also inhibited the hydroxylation of L-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.
Author supplied keywords
Cite
CITATION STYLE
Kubo, I., Chen, Q. X., Nihei, K. I., Calderón, J. S., & Céspedes, C. L. (2003). Tyrosinase Inhibition Kinetics of Anisic Acid. Zeitschrift Fur Naturforschung - Section C Journal of Biosciences, 58(9–10), 713–718. https://doi.org/10.1515/znc-2003-9-1021
Register to see more suggestions
Mendeley helps you to discover research relevant for your work.