Abstract
Fungal tyrosinases and laccases can utilize similar substrates and can be difficult to differentiate. In Agaricus bisporus, both enzymes can use dopa, p-cresol, and diaminobenzidine as substrates, albeit at different rates. Tolidine can be used as a selective substrate to differentiate Agaricus laccase from Agaricus tyrosinase. Oxidation of this substrate, however, did not appear to be inhibited by cetyltrimethylammonium bromide, a common laccase inhibitor. N-hydroxylglycine appeared to be a selective inhibitor of laccase since it did not inhibit tyrosinase activity. Tropolone, salicylhydroxamic acid, and 4-hexylresorcinol were more effective inhibitors of tyrosinase at low concentrations than cinnamic acid or 2,3-naphthalenediol. Similar patterns of substrate and inhibitor preferences were noted in other mushroom species such as Oyster, Enoki, and Shiitake mushrooms.
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