Consecutive polymerization and depolymerization of kraft lignin by Trametes cingulata

Nugzar N. Nutsubidze, Simo Sarkanen, Elmer L. Schmidt, Sheena Shashikanth

Research output: Contribution to journalArticlepeer-review

20 Scopus citations


In extracellular solutions from white-rot fungal cultures, lignin components typically encounter opposing tendencies to be polymerized and depolymerized. The enzymes most commonly purported to bring about lignin depolymerization - lignin peroxidase, manganese-dependent peroxidase and laccase - can all act as single-electron oxidants. Accordingly they may produce from particular lignin monomer residues, either indirectly or directly, phenoxy radicals that will undergo bimolecular coupling, unless they are otherwise preemptively transformed. The present work has sought to elucidate whether discrimination between polymerization and depolymerization is really so precariously established in the progenitorial step of the biodegradative pathway. Some white-rot fungi express no detectable peroxidase activity of any kind and yet degrade lignins very effectively. For the sake of simplicity, one of these, Trametes cingulata, was selected to explore whether there might be some connection between lignin polymerization and depolymerization in vivo. The (Mn-free) culture medium was a multicomponent homogeneous solution containing 0.55 gl-1 softwood kraft lignin, which was adopted as the substrate because of its adequate solubility. As it grew vegetatively, T. cingulata polymerized the dissolved lignin components but then, after cessation of primary growth, the high molecular weight polymerized substrate was completely degraded. No lignin peroxidase or Mn- dependent peroxidase activity was detected in the extracellular culture solution during either metabolic phase, although ('laccase-like') oxidase activity towards 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) (ABTS) persisted throughout the entire process. The results suggest that the overall effect of T. cingulata upon the kraft lignin substrate is governed by the consecutive release of distinct polymerizing and depolymerizing enzymes.

Original languageEnglish (US)
Pages (from-to)1203-1212
Number of pages10
Issue number5
StatePublished - Nov 5 1998

Bibliographical note

Funding Information:
—Support of this work by the Vincent Johnson Lignin Research Fund at the University of Minnesota, the United States Department of Agriculture (Grant 91-37103-6833) and the Minnesota Agricultural Experiment Station is gratefully acknowledged.

Funding Information:
Paper No. 974436801 of the Scientific Journal Series of the Minnesota Agricultural Experiment Station, funded through Minnesota Agricultural Experiment Station Project No. 43-68, supported by Hatch Funds.


  • Kraft lignin
  • Laccase
  • Lignin biodegradation
  • Lignin depolymerase
  • Trametes cingulata
  • White-rot fungus


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