Laccase activity accumulated during rhizomorph development in malt extract cultures of . The activity was readily separated into two bands by PAGE under non-denaturing conditions. The less rapidly migrating activity (on PAGE) was purified by ammonium sulphate precipitation, anion-exchange chromatography and gel filtration. The purified enzyme (laccase I) showed a main polypeptide of 59000. Activity of the purified enzyme was greatest with 2,6-dimethoxyphenol (DMOP) as substrate. Syringaldazine, -phenylenediamine and other typical laccase substrates were readily oxidized. No oxidation of tyrosine was detected. The for DMOP was 0·178 mM and for -phenylenediamine was 1·69 mM. The pH optimum for -phenylenediamine oxidation was 3·5. Electrophoretically purified main polypeptide of laccase I was used to raise a specific antibody. Immunoblot analysis showed that whilst the antibody bound strongly to laccase I, no binding to laccase II was detectable. Antibody raised against pure laccase from reacted with laccase I from but not with laccase II. The isolectric pH was 4.1 for laccase I and 3·3 for laccase II.


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