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. 1990 Jun;56(6):1806–1812. doi: 10.1128/aem.56.6.1806-1812.1990

Mineralization of 14C-Ring-Labeled Synthetic Lignin Correlates with the Production of Lignin Peroxidase, not of Manganese Peroxidase or Laccase

Juana Perez 1,†, Thomas W Jeffries 1,*
PMCID: PMC184514  PMID: 16348221

Abstract

Recently, Mn(II) has been shown to induce manganese peroxidases (MnPs) and repress lignin peroxidases (LiPs) in defined liquid cultures of several white rot organisms. The present work shows that laccase is also regulated by Mn(II). We therefore used Mn(II) to regulate production of LiP, MnP, and laccase activities while determining the effects of Mn(II) on mineralization of ring-labeled synthetic lignin. At a low Mn(II) level, Phanerochaete chrysosporium and Phlebia brevispora produced relatively high titers of LiPs but only low titers of MnPs. At a high Mn(II) level, MnP titers increased 12- to 20-fold, but LiPs were not detected in crude broths. P. brevispora formed much less LiP than P. chrysosporium, but it also produced laccase activity that increased more than sevenfold at the high Mn(II) level. The rates of synthetic lignin mineralization by these organisms were similar and were almost seven times higher at low than at high Mn(II). Increased synthetic lignin mineralization therefore correlated with increased LiP, not with increased MnP or laccase activities.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bonnarme P., Jeffries T. W. Mn(II) Regulation of Lignin Peroxidases and Manganese-Dependent Peroxidases from Lignin-Degrading White Rot Fungi. Appl Environ Microbiol. 1990 Jan;56(1):210–217. doi: 10.1128/aem.56.1.210-217.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bourbonnais R., Paice M. G. Veratryl alcohol oxidases from the lignin-degrading basidiomycete Pleurotus sajor-caju. Biochem J. 1988 Oct 15;255(2):445–450. doi: 10.1042/bj2550445. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Crawford D. L., Crawford R. L. Microbial degradation of lignocellulose: the lignin component. Appl Environ Microbiol. 1976 May;31(5):714–717. doi: 10.1128/aem.31.5.714-717.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Forrester I. T., Grabski A. C., Burgess R. R., Leatham G. F. Manganese, Mn-dependent peroxidases, and the biodegradation of lignin. Biochem Biophys Res Commun. 1988 Dec 30;157(3):992–999. doi: 10.1016/s0006-291x(88)80972-0. [DOI] [PubMed] [Google Scholar]
  5. Glenn J. K., Gold M. H. Purification and characterization of an extracellular Mn(II)-dependent peroxidase from the lignin-degrading basidiomycete, Phanerochaete chrysosporium. Arch Biochem Biophys. 1985 Nov 1;242(2):329–341. doi: 10.1016/0003-9861(85)90217-6. [DOI] [PubMed] [Google Scholar]
  6. Glenn J. K., Morgan M. A., Mayfield M. B., Kuwahara M., Gold M. H. An extracellular H2O2-requiring enzyme preparation involved in lignin biodegradation by the white rot basidiomycete Phanerochaete chrysosporium. Biochem Biophys Res Commun. 1983 Aug 12;114(3):1077–1083. doi: 10.1016/0006-291x(83)90672-1. [DOI] [PubMed] [Google Scholar]
  7. Hammel K. E., Tien M., Kalyanaraman B., Kirk T. K. Mechanism of oxidative C alpha-C beta cleavage of a lignin model dimer by Phanerochaete chrysosporium ligninase. Stoichiometry and involvement of free radicals. J Biol Chem. 1985 Jul 15;260(14):8348–8353. [PubMed] [Google Scholar]
  8. Jeffries T. W., Choi S., Kirk T. K. Nutritional Regulation of Lignin Degradation by Phanerochaete chrysosporium. Appl Environ Microbiol. 1981 Aug;42(2):290–296. doi: 10.1128/aem.42.2.290-296.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kawai S., Umezawa T., Higuchi T. Degradation mechanisms of phenolic beta-1 lignin substructure model compounds by laccase of Coriolus versicolor. Arch Biochem Biophys. 1988 Apr;262(1):99–110. doi: 10.1016/0003-9861(88)90172-5. [DOI] [PubMed] [Google Scholar]
  10. Kersten P. J., Tien M., Kalyanaraman B., Kirk T. K. The ligninase of Phanerochaete chrysosporium generates cation radicals from methoxybenzenes. J Biol Chem. 1985 Mar 10;260(5):2609–2612. [PubMed] [Google Scholar]
  11. Keyser P., Kirk T. K., Zeikus J. G. Ligninolytic enzyme system of Phanaerochaete chrysosporium: synthesized in the absence of lignin in response to nitrogen starvation. J Bacteriol. 1978 Sep;135(3):790–797. doi: 10.1128/jb.135.3.790-797.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kirk T. K., Connors W. J., Bleam R. D., Hackett W. F., Zeikus J. G. Preparation and microbial decomposition of synthetic [14C]ligins. Proc Natl Acad Sci U S A. 1975 Jul;72(7):2515–2519. doi: 10.1073/pnas.72.7.2515. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kirk T. K., Farrell R. L. Enzymatic "combustion": the microbial degradation of lignin. Annu Rev Microbiol. 1987;41:465–505. doi: 10.1146/annurev.mi.41.100187.002341. [DOI] [PubMed] [Google Scholar]
  14. Niku-Paavola M. L., Karhunen E., Salola P., Raunio V. Ligninolytic enzymes of the white-rot fungus Phlebia radiata. Biochem J. 1988 Sep 15;254(3):877–883. doi: 10.1042/bj2540877. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Paszczyński A., Huynh V. B., Crawford R. Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium. Arch Biochem Biophys. 1986 Feb 1;244(2):750–765. doi: 10.1016/0003-9861(86)90644-2. [DOI] [PubMed] [Google Scholar]
  16. Tien M., Kirk T. K. Lignin-Degrading Enzyme from the Hymenomycete Phanerochaete chrysosporium Burds. Science. 1983 Aug 12;221(4611):661–663. doi: 10.1126/science.221.4611.661. [DOI] [PubMed] [Google Scholar]
  17. Wariishi H., Akileswaran L., Gold M. H. Manganese peroxidase from the basidiomycete Phanerochaete chrysosporium: spectral characterization of the oxidized states and the catalytic cycle. Biochemistry. 1988 Jul 12;27(14):5365–5370. doi: 10.1021/bi00414a061. [DOI] [PubMed] [Google Scholar]

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