Publication | Closed Access
Studies on the Laccase of Lentinus edodes: Specificity, Localization and Association with the Development of Fruiting Bodies
194
Citations
22
References
1981
Year
BiologyLaccase ActivityBiosynthesisMajor Phenol OxidaseBiochemistryBotanyNatural SciencesEvolutionary BiologyMicrobiologyRipeningFruiting BodiesPhytochemistryPhytochemicalLentinus Edodes
The phenol oxidases from mature fruiting bodies of Lentinus edodes (Berk.) Sing., a commercially cultivated mushroom, were studied. The major phenol oxidase was a laccase with a pH optimum near 4.0 and an apparent molecular weight of 100000. Catechol oxidase and tyrosinase were also present. The laccase investigated was primarily extracellular; the highest activity was in the pigmented rind of the pileus and in the stipe. Increased laccase activity was associated with rapid growth of non-pigmented aerial mycelium and formation of pigmented primordia and fruiting bodies. Possible functions of the laccase and its regulation during the development of fruiting bodies are discussed.
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