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Multiple lignin peroxidases of Phanerochaete chrysosporium INA-12.

Authors
  • Odier, E1
  • Delattre, M
  • 1 Laboratoire de Microbiologie, Centre de Biotechnologies Agro-Industrielles, Thiverval-Grignon, France. , (France)
Type
Published Article
Journal
Enzyme and Microbial Technology
Publisher
Elsevier
Publication Date
Jun 01, 1990
Volume
12
Issue
6
Pages
447–452
Identifiers
PMID: 1366630
Source
Medline
License
Unknown

Abstract

Nine proteins with lignin peroxidase activity were separated from cultures of Phanerochaete chrysosporium INA-12 in glycerol as carbon source and non-nitrogen limited. Four lignin peroxidase isozymes (4, 5, 8, 9) were purified and characterized. Although differences in kinetic parameters could be shown, antibody reaction showed homology between isozymes. However, thermal stability studied, peptide mapping results, and N-terminal sequence analyses established a higher degree of homology between isozymes 4/5 and 8/9 types. Protein characterization and kinetic data indicate that lignin peroxidase isozymes 4, 5, 8, and 9 differ from described isozymes in strain BKM. The higher specific activity of lignin peroxidase isozymes in cultures with glycerol than in nitrogen-starved cultures accounts for the higher lignin peroxidase activity obtained in these conditions.

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