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Characterization of a laccase secreted by Armillaria mellea pathogenic for Genista



Characterization of a laccase secreted by Armillaria mellea pathogenic for Genista



Plant Physiology & Biochemistry 35(2): 147-153



A laccase has been purified with high yields and characterised from the in vitro culture medium of Armillaria mellea. The enzyme has an apparent molecular mass of 80 kDa, and it appears as a single band on PAGE electrophoresis. Under denaturing conditions, the enzyme gives two new bands on PAGE, with molecular masses of about 30 and 40 kDa respectively. The UV-visible spectrum demonstrates the presence of type I and type III copper. The total content of copper is four atoms per molecule of enzyme, and the carbohydrate content is high (37-40%). The isoelectric point is low, around 3. 1. The enzyme oxidises a range of different phenolic substrates typical for fungal laccases. Moreover, the ability of this laccase to oxidise the reduced form of iron may account for a competition for this metal with the plant tissues during growth of the fungus within the host.

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