Improving Bacillus licheniformis Laccase Expression
Author Information
Author(s): Koschorreck Katja, Schmid Rolf D, Urlacher Vlada B
Primary Institution: Institute of Technical Biochemistry, Universitaet Stuttgart
Hypothesis
Can random and site-directed mutagenesis improve the functional expression and activity of Bacillus licheniformis laccase?
Conclusion
The double mutant K316N/D500G of Bacillus licheniformis CotA laccase shows significantly improved expression and activity, making it suitable for biotechnological applications.
Supporting Evidence
- The K316N/D500G double mutant had an 11.4-fold higher expression level than the wild-type.
- The double mutant was more efficient in decolorizing industrial dyes compared to the wild-type.
- Random mutations led to a significant increase in enzyme activity for certain substrates.
Takeaway
Scientists changed some parts of a laccase enzyme to make it work better, which could help in cleaning up pollution and making products.
Methodology
Random and site-directed mutagenesis were used to create and analyze various CotA mutants in E. coli.
Limitations
The study primarily focused on a limited number of mutations and their effects on enzyme activity.
Digital Object Identifier (DOI)
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