Comparison of different microbial laccases as tools for industrial uses

• Laccases are used as lignin-degrading enzymes.
• Biochemical properties of ten laccases under identical conditions were investigated.
• Bacterial laccases retained high activity in DMSO and Tween-80.
• Properties of recombinant B. licheniformis laccase satisfy requirements for industrial uses.

Laccases from different sources are employed in a number of biotechnological processes, each characterized by specific reaction constraints and thus requiring an enzyme with suitable properties. In order to avoid the bias generated by different assay methodologies, in this work we investigated the main properties of ten laccases from fungi and bacteria under identical conditions. As a general rule, the optimal activity was apparent at pH 3–4 and was lost at pH ≥ 7.0 (all laccases were stable at pH ≥ 7.0); enzymes active at neutral pH values were also identified. For all tested laccases, activity increased with temperature up to 80°C and stability was good at 25°C. Interestingly, laccases insensitive to high salt concentration were identified, this favoring their use in treating waste waters. Indeed, bacterial laccases retained a significant activity in the presence of DMSO (up to 40% final concentration) and of surfactants, suggesting that they can be applied in lignin degradation processes requiring solvents. The available laccases are versatile and satisfy requirements related to different processes. Notably, the recombinant laccase from Bacillus licheniformis favorably compares with the tested enzymes, indicating that it is well suited for different biotechnological applications.

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