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Laccase is essential for lignin degradation by the white‐rot fungus Pycnoporus cinnabarinus
Author(s) -
Eggert Claudia,
Temp Ulrike,
Eriksson Karl-Erik L.
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00301-3
Subject(s) - laccase , lignin , fungus , mutant , biochemistry , biology , enzyme , chemistry , botany , gene
The white‐rot fungus, Pycnoporus cinnabarinus , provides an excellent model organism to elucidate the controversial role of laccase in lignin degradation. P. cinnabarinus produces laccase in one isoform as the predominant phenoloxidase in ligninolytic cultures, and neither LiP nor MnP are secreted. Yet, P. cinnabarinus degrades lignin very efficiently. In the present work, we show that laccase‐less mutants of P. cinnabarinus were greatly reduced in their ability to metabolize 14 C ring‐labeled DHP. However, 14 CO 2 evolution in these mutant cultures could be restored to levels comparable to those of the wild‐type cultures by addition of purified P. cinnabarinus laccase. This clearly indicates that laccase is absolutely essential for lignin degradation by P. cinnabarinus .