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Ha, T.J. et al.

Effects of mushroom tyrosinase on anisaldehyde.

Anisaldehyde (p-methoxybenzaldehyde) was previously reported to inhibit the tyrosinase-catalyzed oxidation of L-3,4-dihydroxyphenylalanine (L-DOPA) noncompetitively as long as the enzyme activity was monitored by measuring dopachrome formation. However, anisaldehyde did not inhibit this oxidation if a longer reaction time was observed, although it suppressed the initial rate of oxidation to a certain extent. Anisaldehyde significantly suppressed the rate of enzymatic oxidation of L-tyrosine.[1]

References

Effects of mushroom tyrosinase on anisaldehyde. Ha, T.J., Tamura, S., Kubo, I. J. Agric. Food Chem. (2005) [Pubmed]

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