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Mycologia, 95(6), 2003, pp. 1013-1020.
© 2003 by The Mycological Society of America

The white-rot fungus Pleurotus ostreatus secretes laccase isozymes with different substrate specificities


Mariana Mansur

     Instituto Cubano de Investigaciones de los Derivados de la Caña de Azúcar (ICIDCA), Vía Blanca 804, P.O. Box 4026, La Habana, Cuba

María E. Arias
José L. Copa-Patiño

     Departamento de Microbiología y Parasitología, Universidad de Alcalá, Alcalá de Henares, 28871 Madrid, España

María Flärdh
Aldo E. González 1

     Centro de Investigaciones Biológicas, CSIC, Velázquez 144, 28006 Madrid, España

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.

Key words: ABTS, guaiacol, isozyme, N-terminal sequence, Pleurotus, phenoloxidase






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Copyright © 2003 by The Mycological Society of America.