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Peroxidase and laccase activities in mycorrhizal and non-mycorrhizal fine roots of Norway spruce and larch



Peroxidase and laccase activities in mycorrhizal and non-mycorrhizal fine roots of Norway spruce and larch



Canadian Journal of Botany 75(6): 932-938



Peroxidase (EC 1.11.1.7) and laccase (EC 1.10.3.1) activities were determined in mycorrhizal and non-mycorrhizal main and lateral roots of Picea abies (L.) Karst. (Norway spruce) and Larix decidua Mill. (larch) and in mycelia of the ectomycorrhizal fungus Laccaria amethystea (Bull.) Murr. grown under axenic conditions. Peroxidase isozyme patterns were identified after isoelectric focussing. In both tree species, mycorrhizae contained the lowest, and laterals of noninoculated plants the highest, peroxidase activities. Pure mycelia of Laccaria amethystea contained considerable laccase activity but no peroxidase activity. Laccase activity was barely detected in noninoculated laterals of spruce, but was present in noninoculated laterals of larch and in main roots of Norway spruce and larch. Highest laccase activities were found in mycorrhizae of both tree species, indicating that most of the activity was derived from the fungus. Laterals of Norway spruce contained eight, and those of larch five, acidic peroxidase isozymes. In mycorrhizae of Norway spruce and larch, specific peroxidase isozymes with pI values of 4.5 and 6.2 and 5.8 and 6.0, respectively, were almost completely suppressed. The specific suppression of peroxidase suggests that the fungal symbiont is able to modify the host defence response in mature mycorrhizae.

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