, Volume 190, Issue 1, pp 75–87 | Cite as

Extracellular laccases and peroxidases from sycamore maple (Acer pseudoplatanus) cell-suspension cultures

Reactions with monolignols and lignin model compounds
  • Raja Sterjiades
  • Jeffrey F. D. Dean
  • Gary Gamble
  • David S. Himmelsbach
  • Karl-Erik L. Eriksson


We have investigated the abilities of extracellular enzymes from dark-grown cell-suspension cultures of sycamore maple (Acer pseudoplatanus L.) to oxidize monolignols, the precursors for lignin biosynthesis in plants, as well as a variety of other lignin-related compounds. Laccase and peroxidase both exist as a multiplicity of isoenzymes in filtrates of spent culture medium, but their abilities to produce water-insoluble, dehydrogenation polymers (DHPs) from the monolignols (in the presence of hydrogen peroxide for the peroxidase reaction) appear identical whether or not the enzymes are purified from the concentrated filtrates or left in a crude mixture. The patterns of bonds formed in these DHPs are identical to those found in DHPs synthesized using horseradish peroxidase or fungal laccase, and many of these bonds are found in the natural lignins extracted from different plant sources. On the other hand, sycamore maple laccase is very much less active on phenolic substrates containing multiple aromatic rings than is sycamore maple peroxidase. We suggst that whereas laccase may function during the early stages of lignification to polymerize monolignols into oligo-lignols, cell-wall peroxidases may function when H2O2 is produced during the later stages of xylem cell development or in response to environmental stresses.

Key words

Acer (lignin biosynthesis) Cell wall p-Diphenol: O2 oxidoreductase Lignification Phenolox idase 



dehydrogenation polymer


isoelectric focuring


nuclear magnetic resonance


polyacrylamide gel electrophoresis


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Copyright information

© Springer-Verlag 1993

Authors and Affiliations

  • Raja Sterjiades
    • 1
  • Jeffrey F. D. Dean
    • 1
  • Gary Gamble
    • 2
  • David S. Himmelsbach
    • 2
  • Karl-Erik L. Eriksson
    • 1
  1. 1.Department of BiochemistryCenter for Biological Resource Recovery, University of GeorgiaAthensUSA
  2. 2.US Department of AgricultureRichard B. Russell Agricultural Research Center, Agricultural Research ServiceAthensUSA

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