Competitive Inhibition of Mushroom Tyrosinase by 4-Substituted Benzaldehydes

ArticleinJournal of Agricultural and Food Chemistry 49(8):4060-3 · September 2001with27 Reads
Impact Factor: 2.91 · DOI: 10.1021/jf010194h · Source: PubMed


    A kinetic study of the inhibition of mushroom tyrosinase by 4-substituted benzaldehydes showed that these compounds behave as classical competitive inhibitors, inhibiting the oxidation of L-3,4-dihydroxyphenylalanine (L-DOPA) by mushroom tyrosinase (o-diphenolase activity). The kinetic parameter (K(I)) characterizing this inhibition was evaluated for all of the seven compounds assayed. Cuminaldehyde showed the most potent inhibitory activity (K(I) = 9 microM). It also inhibited the oxidation of L-tyrosine by mushroom tyrosinase (o-monophenolase activity) in a competitive manner. The corresponding kinetic parameter for this inhibition was evaluated (K(I) = 0.12 mM).