Peroxidase activity can dictate the in vitro lignin dehydrogenative polymer structure

Phytochemistry. 2007 Feb;68(4):571-9. doi: 10.1016/j.phytochem.2006.11.024. Epub 2006 Dec 21.

Abstract

The objective of this study was to assess the influence of the peroxidase/coniferyl alcohol (CA) ratio on the dehydrogenation polymer (DHP) synthesis. The soluble and unsoluble fractions of horseradish peroxidase (HRP)-catalyzed CA dehydrogenation mixtures were recovered in various proportions, depending on the polymerization mode (Zutropf ZT/Zulauf ZL) and HRP/CA ratio (1.6-1100purpurogallin U mmol(-1)). The ZL mode yielded 0-57%/initial CA of unsoluble condensed DHPs (thioacidolysis yields <200micromolg(-1)) with a proportion of uncondensed CA end groups increasing with the HRP/CA ratio (7.2-55.5%/total uncondensed CA). Systematically lower polymer yields (0-49%/initial CA) were obtained for the ZT mode. In that mode, a negative correlation was established between the beta-O-4 content (thioacidolysis yields: 222-660micromolg(-1)) and the HRP/CA ratio. In both modes, decreasing the HRP/CA ratio below 18Ummol(-1) favoured an end-wise polymerization process evidenced by the occurrence of tri-, tetra- and pentamers involving at least one beta-O-4 bond. At low ratio, the unsoluble ZT DHP was found to better approximate natural lignins than DHPs previously synthesized with traditional methods. Besides its possible implication in lignin biosynthesis, peroxidase activity is a crucial parameter accounting for the structural variations of in vitro DHPs.

MeSH terms

  • Benzocycloheptenes / metabolism
  • Chromatography, Liquid
  • Horseradish Peroxidase / metabolism*
  • Kinetics
  • Lignin / chemistry*
  • Lignin / metabolism*
  • Mass Spectrometry
  • Oxidation-Reduction

Substances

  • Benzocycloheptenes
  • Lignin
  • Horseradish Peroxidase
  • purpurogallin