Paper
Competitive inhibition of mushroom tyrosinase by 4-substituted benzaldehydes.
Published Jul 21, 2001 · M. Jiménez, S. Chazarra, J. Escribano
Journal of agricultural and food chemistry
141
Citations
2
Influential Citations
Abstract
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).
In Vitro Study
Highly Cited4-substituted benzaldehydes effectively inhibit mushroom tyrosinase, with cuminaldehyde showing the most potent inhibitory activity.
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