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Abstract
Four laccase isozymes (LCC1, LCC2, LCC3 and LCC4) synthesized by Pleurotus ostreatus strain V-184 were purified and characterized. LCC1 and LCC2 have molecular masses of about 60 and 65 kDa and exhibited the same pI value (3.0). Their N termini were sequenced, revealing the same amino acid sequence and homology with laccases from other microorganisms. Laccases LCC3 and LCC4 were characterized by SDS-PAGE, estimating their molecular masses around 80 and 82 kDa, respectively. By native isoelectrofocusing, their pI values were 4.7 and 4.5, respectively. When staining with ABTS and guaiacol in native polyacrilamide gels, different specificities were observed for LCC1/LCC2 and LCC3/LCC4 isozymes.
We thank A. D. W. Dobson, G. del Solar and M. C. Terrón for critically reading the manuscript. M. Mansur acknowledges support from fellowships granted by the Instituto de Cooperación Iberoamericano and Dirección de Relaciones Internacionales del Consejo Superior de Investigaciones Científicas, España. This work was supported by Grant BIO 93-0662-CO4-01 (CICYT, España).
