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Thermotolerant and thermostable laccases
Kristiina Hildén1, Terhi K Hakala, Taina Lundell
1Department of Applied Chemistry and Microbiology, Viikki Biocenter, University of Helsinki, Helsinki, Finland. kristiina.s.hilden@helsinki.fi
Biotechnology Letters
|April 11, 2009
Summary
This review focuses on fungal laccases, which are copper-containing enzymes used in various industrial applications. It highlights the need for enhanced laccases with improved thermostability for novel biocatalytic processes.
Area of Science:
- Biochemistry
- Enzymology
- Biotechnology
Background:
- Laccases are copper-containing metalloenzymes that oxidize phenols.
- They are widely used in industrial applications like beverage processing, wastewater treatment, and lignin modification.
- Current applications require laccases with improved biochemical properties, particularly thermostability.
Purpose of the Study:
- To provide an overview of fungal laccases.
- To discuss sources and characteristics of thermostable laccases.
- To emphasize the importance of enhanced laccase properties for biocatalysis.
Main Methods:
- Literature review of fungal laccases.
- Analysis of enzyme characteristics, focusing on thermostability.
- Identification of sources for improved laccase variants.
Main Results:
- Fungal laccases are versatile biocatalysts with significant industrial potential.
- Thermostability is a key property for expanding laccase applications.
- Various fungal sources offer laccases with desirable biochemical traits.
Conclusions:
- Enhanced fungal laccases are crucial for developing efficient biocatalytic processes.
- Further research into laccase sources and engineering is needed.
- Optimized laccases will drive innovation in biotechnology and industry.
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