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.