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Benzaldehyde inhibited the oxidation of 4-t-butylcatechol catalyzed by mushroom tyrosinase with an IC50 of 31.0 μM. The inhibition kinetics analyzed by Dixon plot indicated that it acts as a partial noncompetitive inhibitor. Further studies of several benzaldehydes, particularly those having a substitution at C-4, suggested that the partial inhibitory property diminished when using a bulk substituent. For example, 4-penthylbenzaldehyde showed a full and mixed type inhibition on diphenolase activity. Therefore, 4-substituted benzaldehyde on the aromatic ring primarily reflected the rate of product formation as it may act as a tight hydrophobic cover on the catalytic center of tyrosinase. Copyright © 2017 Elsevier Masson SAS. All rights reserved.


Ken-Ichi Nihei, Isao Kubo. Substituent effect of benzaldehydes on tyrosinase inhibition. Plant physiology and biochemistry : PPB. 2017 Mar;112:278-282

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PMID: 28119115

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