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Low pH dye decolorization with ascomycete Lamprospora wrightii laccase.
Kitti Mueangtoom1, Roman Kittl, Oliver Mann
1Department of Food Sciences and Technology, University of Natural Resources and Applied Life Sciences, Vienna, Austria.
Biotechnology Journal
|July 24, 2010
Summary
Researchers identified a potent laccase enzyme from the fungus Lamprospora wrightii, demonstrating high efficiency in decolorizing various industrial dyes. This enzyme shows promise for bioremediation applications in acidic environments.
Area of Science:
- Enzymology
- Mycology
- Biotechnology
Background:
- Laccase enzymes are frequently found in various ascomycetes.
- Lamprospora wrightii, a moss-associated fungus, was identified as a high laccase producer.
Purpose of the Study:
- To characterize the laccase from the saprotrophic ascomycete Lamprospora wrightii.
- To evaluate its potential for bioremediation, particularly in acidic conditions.
Main Methods:
- Screening of ascomycetes for laccase activity.
- Optimization of laccase expression using tomato juice or copper sulfate.
- Purification and characterization of the laccase enzyme.
- Assessing dye decolorization efficiency at different pH levels.
Main Results:
- Laccase expression in L. wrightii was enhanced by specific medium additives, reaching 420 U/mL.
- The purified laccase (68 kDa, pI 3.4) exhibited properties similar to basidiomycete laccases.
- The enzyme showed excellent activity and stability at low pH.
- Ten tested dyes were decolorized, with five showing very efficient degradation, involving chromophore breakdown and polymerization.
Conclusions:
- Laccase from L. wrightii is a robust enzyme with potential for industrial dye bioremediation in acidic environments.
- Its catalytic properties and stability make it a valuable candidate for environmental applications.
