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Laccase from Sycamore Maple (Acer pseudoplatanus) Polymerizes Monolignols
R Sterjiades1, J F Dean, K E Eriksson
1Department of Biochemistry, Center for Biological Resource Recovery, University of Georgia, Athens, Georgia 30602.
Plant Physiology
|July 1, 1992
Summary
Sycamore maple laccase enzyme aids in lignin deposition by polymerizing monolignols. This study purified and characterized sycamore maple laccase, confirming its role in forming lignin polymers.
Area of Science:
- Plant biochemistry
- Enzymology
Background:
- Lignin deposition in plants is crucial for structural integrity.
- The specific enzymes, localization, and regulation of lignin biosynthesis remain incompletely understood.
- Laccase is a potential enzyme involved in catalyzing monolignol polymerization.
Purpose of the Study:
- To investigate the role of laccase in lignin deposition in sycamore maple (Acer pseudoplatanus).
- To purify and characterize sycamore maple laccase.
- To determine the activity of purified laccase on monolignol substrates.
Main Methods:
- Utilized sycamore maple cell suspension cultures.
- Determined laccase secretion time course.
- Purified laccase using hydrophobic interaction column chromatography.
- Assessed enzyme purity via gel electrophoresis techniques.
- Performed amino acid, glycosyl, and specific activity analyses.
Main Results:
- Successfully secreted and purified laccase from sycamore maple cell cultures.
- Confirmed laccase purity through multiple electrophoresis methods.
- Demonstrated that sycamore maple laccase oxidizes sinapyl, coniferyl, and p-coumaryl alcohols.
- Observed the formation of water-insoluble dehydrogenation polymers from these alcohols.
Conclusions:
- Sycamore maple laccase is effectively secreted into the extracellular matrix.
- The purified enzyme exhibits activity towards key monolignols, producing lignin-like polymers.
- This provides strong evidence for laccase's role in the final oxidative steps of lignin biosynthesis in plants.