Applied Microbiology and Biotechnology

, Volume 45, Issue 3, pp 399–403

Laccase activities of Penicillium chrysogenum in relation to lignin degradation

  • A. Rodríguez
  • M. A. Falcón
  • A. Carnicero
  • F. Perestelo
  • G. De la Fuente
  • J. Trojanowski
ORIGINAL PAPER

DOI: 10.1007/s002530050702

Cite this article as:
Rodríguez, A., Falcón, M., Carnicero, A. et al. Appl Microbiol Biotechnol (1996) 45: 399. doi:10.1007/s002530050702

Abstract

 An extracellular laccase capable of oxidizing ABTS (the diammonium salt of 2,2′-azinobis-3-ethylbenzothiazoline-6-sulfonic acid) was detected in ligninolytic cultures of Penicillium chrysogenum. By contrast, no lignin peroxidase, manganese-dependent peroxidase or aryl-alcohol oxidase was detected at any time during culturing. Both ABTS laccase activity and mineralization of dehydrogenative polymerizate of coniferyl alcohol were regulated by the C/N ratio in the medium and partially inhibited in the presence of thioglycolic acid, suggesting that both events are associated. In the presence of several known laccase inducers neither ABTS laccase activity nor mineralization rates were enhanced. However, a new laccase was detected in P. chrysogenum, able to oxidize 2,6-dimethoxyphenol but not involved in lignin mineralization. Studies with the known ligninolytic basidiomycete Trametes villosa suggest that lignin degradation by this fungus also involves the action of laccase.

Copyright information

© Springer-Verlag Berlin Heidelberg 1996

Authors and Affiliations

  • A. Rodríguez
    • 1
  • M. A. Falcón
    • 1
  • A. Carnicero
    • 1
  • F. Perestelo
    • 1
  • G. De la Fuente
    • 2
  • J. Trojanowski
    • 3
  1. 1.Departamento de Microbiología y Biología Celular, Facultad de Farmacia, Universidad de La Laguna, 38206 La Laguna, Tenerife, SpainES
  2. 2.Instituto de Productos Naturales y Agrobiología del CSIC, 38206 La Laguna, Tenerife, SpainES
  3. 3.Forstbotanisches Institut der Universität Göttingen, Büsgenweg 2, D-37077 Göttingen, GermanyDE