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Sigma's Non-specific Protease Activity Assay - Casein as a Substrate
Published on: September 17, 2008
Tyrosinase inhibition kinetics of anisic acid
Isao Kubo1, Qing-Xi Chen, Ken-Ichi Nihei
1Department of Environmental Science, Policy and Management, University of California, Berkeley, California 94720-3112, USA. ikubo@uclink4.berkeley.edu
Abstract:
Anisic acid (p-methoxybenzoic acid) was characterized as a tyrosinase inhibitor from ani-seed, a common food spice. It inhibited the oxidation of L-3,4-dihydroxyphenylalanine (L-DOPA) catalyzed by tyrosinase with an IC50 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.
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