Agaricus bisporus browning is a common and economically detrimental phenomenon, in which melanogenic phenols are enzymically processed into quinones, which evolve eventually to melanins. This review deals with the two fundamental sides of this process, enzyme(s) and phenolic substrates. Mushroom tyrosinase, the main polyphenol oxidase encountered in the A. bisporus sporophore, is treated in the first part. Its overall molecular architecture, isoforms, primary sequence and genetic background are considered. The presentation of tyrosinase catalytic features, including enzyme assays, kinetic properties, substrates and inhibitors, is followed by a comprehensive description of the active site and reaction mechanisms. Because of their relevance for studies of mushroom browning during development and post-harvest storage, the occurrence and properties of latent enzyme forms, as well as the location of tyrosinase and variations of its activity during the A. bisporus life cycle, are also reviewed. The second part deals with the substrates, particularly γ-L-glutaminyl-4-hydroxybenzene (GHB) and its derivatives. Main data concerning the nature, obtention (by extraction or synthesis), spectrometric and chromatographic characteristics, chemical stabilities and biological properties of these typical Agaricaceae compounds are presented. Their distribution and levels according to the strains and flushes are described, as well as their variations during storage. Thirdly, the relationship between browning and the natural or pathogenic discolouration intensity is developed.
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