Discrimination between alternative substrates and inhibitors of tyrosinase

J Agric Food Chem. 2015 Mar 4;63(8):2162-71. doi: 10.1021/jf5051816. Epub 2015 Feb 18.

Abstract

Many phenolic compounds have been described in the scientific literature as inhibitors of tyrosinase. In this work a test is proposed that allows us to distinguish whether a molecule is an enzyme inhibitor or substrate. The test has several stages. First, the degree of inhibition of the studied molecule is determined on the monophenolase activity (i(M)) and on the diphenolase activity (i(D)). If i(M) = i(D), it is an inhibitor. If i(M) ≠ i(D), the molecule could be substrate or inhibitor. Several additional stages are proposed to solve this ambiguity. The study described herein was carried out using the following molecules: benzoic acid, cinnamic acid, guaiacol, isoeugenol, carvacrol, 4-tert-butylphenol, eugenol, and arbutin.

Keywords: degree of inhibition; inhibitor; kinetic; polyphenol oxidase; substrate; tyrosinase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agaricales / enzymology*
  • Discriminant Analysis
  • Enzyme Inhibitors / chemistry*
  • Fungal Proteins / chemistry*
  • Kinetics
  • Monophenol Monooxygenase / chemistry*
  • Phenols / chemistry*
  • Substrate Specificity

Substances

  • Enzyme Inhibitors
  • Fungal Proteins
  • Phenols
  • Monophenol Monooxygenase