Introduction Microbial degradation of lignin is mainly accomplished by basidiomycetes. In nature, the biodegradation of lignin is the rate-limiting step of the overall carbon cycle. The microbial degradation is catalyzed by enzymes, which can be produced under suitable conditions in bioreactors. Since the discovery of the first lignin peroxidase enzyme in the culture broth of Phanerochaete chrysosporium (Tien and Kirk 1983; Glenn et al. 1983), the application of ligninmodifying enzymes especially in the pulp and paper industry has attracted great interest. Low production levels have limited the use of lignin-modifying enzymes on polymeric lignin substrates. Production methods for lignin-modifying enzymes have recently been improved (Linko 1988; Kantelinen et al. 1989; Polvinen et al. 1991) but for possible large-scale applications, cloning of these enzymes to more efficient production hosts is inevitable. Hithertp laccase is the only lignin-modifying enzyme which has been expressed in active form when cloned to another eukaryote (Saloheimo and Niku-Paavola 1991). Characterization of the reactions catalyzed by ligninmodifying enzymes has usually been carried out with low molecular mass lignin model compounds. Only a few reports have been published of studies concerning polymeric, native or synthetic and industrial lignins. Both depolymerization and polymerization have been To whom
Holzforschung - International Journal of the Biology, Chemistry, Physics and Technology of Wood – de Gruyter
Published: Jan 1, 1993
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