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Modelling, docking and simulation analysis of Bisphenol A interaction with laccase from Trichoderma.

Sankar Ganesh Ramakrishnan¹, Muthusaravanan Sivaramakrishnan², Dhrisya Chenthamara¹

¹Department of Microbial Biotechnology, Bharathiar University, Coimbatore, India.

|August 11, 2020

Summary

Fungal laccases can degrade harmful chemicals. This study shows Trichoderma laccase effectively binds to Bisphenol A, a common endocrine-disrupting chemical, indicating potential for bioremediation.

Keywords:

Bisphenol-A Laccase docking molecular simulation

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Area of Science:

Biochemistry and Environmental Science
Enzymology and Xenobiotic Degradation

Background:

Fungal laccases are crucial enzymes for breaking down persistent environmental pollutants.
Endocrine-Disrupting Chemicals (EDCs) like Bisphenol A pose significant environmental and health risks.
Understanding enzyme-pollutant interactions is key to developing bioremediation strategies.

Purpose of the Study:

To investigate the binding interaction between fungal laccase from Trichoderma laccase and Bisphenol A.
To assess the potential of Trichoderma laccase in degrading Bisphenol A.

Main Methods:

Molecular docking analysis was employed to simulate the interaction.
Laccase from Trichoderma laccase was docked with Bisphenol A and 23 other xenobiotic compounds.
Binding affinity was evaluated using Glide score and Glide energy.

Main Results:

Bisphenol A exhibited optimal binding characteristics with laccase from Trichoderma laccase.
The molecular docking revealed a Glide score of -5.44 and Glide energy of -37.65 kcal/mol for Bisphenol A.
These results suggest a strong interaction between the enzyme and the EDC.

Conclusions:

Trichoderma laccase demonstrates significant binding affinity for Bisphenol A.
The enzyme shows potential as a biocatalyst for the degradation of this endocrine-disrupting chemical.
Further studies are warranted to explore the practical application of Trichoderma laccase in Bisphenol A bioremediation.