Isolation, Purification, and Characterization of Fungal Laccase from Pleurotus sp.
2011
Isolation and Characterization of Laccase from Pleurotus sp.
Sample size: 28
publication
10 minutes
Evidence: moderate
Author Information
Author(s): Sunil S. More, P. S. Renuka, K. Pruthvi, M. Swetha, Malini S., S. M. Veena
Primary Institution: Jain University
Hypothesis
The study aims to isolate and characterize laccase-producing fungi from soil samples.
Conclusion
The laccase from Pleurotus sp. was successfully purified and characterized, showing potential for industrial applications.
Supporting Evidence
- The purified laccase showed a molecular mass of 40 ± 1 kDa.
- The enzyme exhibited optimal activity at pH 4.5 and 65°C.
- Laccase activity reached a maximum of 112.88 U/mL at pH 6.5 without inducer.
- The purification process resulted in a 72-fold increase in enzyme purity.
- Metal ions like CuSO4 and BaCl2 did not significantly affect laccase activity.
- Sodium azide was found to be a potent inhibitor of laccase activity.
- The K_m and V_max values for ABTS were 250 mM and 0.33 μmol/min, respectively.
- The study identified a new source of extracellular laccase from Pleurotus sp.
Takeaway
Scientists found a special enzyme called laccase from a type of mushroom that can help clean up pollution.
Methodology
The laccase was isolated from soil samples, purified using ion-exchange and gel filtration chromatography, and characterized for its activity and stability.
Limitations
The study does not address the scalability of laccase production for industrial applications.
Digital Object Identifier (DOI)
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