Excellent Degradation Performance of a Versatile Phthalic Acid Esters-Degrading Bacterium and Catalytic Mechanism of Monoalkyl Phthalate Hydrolase
Abstract
:1. Introduction
2. Results and Discussion
2.1. Excellent DEHP-Degrading Performance of Strain YC-JH1
2.2. Catabolic Pathway of DEHP by Strain YC-JH1
2.3. Sequence and Activity Analysis of MphG1
2.4. Interaction Mode of MphG1-MAP Complex
2.5. The Mutation Analysis and Catalytic Mechanism of MphG1
3. Materials and Methods
3.1. Chemicals, Medium and Strain
3.2. DEHP Degradation Assay by Strain YC-JH1
3.3. Identification of Intermediates of DEHP Degradation
3.4. Gene Cloning, Expression and Purification of Enzyme
3.5. Hydrolase Activity Assay
3.6. Molecular Docking and Molecular Dynamics Simulation
4. Conclusions
Supplementary Materials
Author Contributions
Funding
Acknowledgments
Conflicts of Interest
References
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Substrate | Structure | Binding Energy (kcal/mol) | Specific Activity (U/mg) |
---|---|---|---|
MEP | −7.86 | 2.84 ± 0.14 | |
MBP | −9.20 | 2.99 ± 0.04 | |
MHP | −17.34 | 3.14 ± 0.06 | |
MEHP | −13.72 | 2.91 ± 0.09 |
Complex | RMSD/Å |
---|---|
MphG1-MEP | 3.3774 ± 0.4 |
MphG1-MBP | 3.2302 ± 0.4 |
MphG1-MHP | 3.4007 ± 0.4 |
MphG1-MEHP | 3.4492 ± 0.3 |
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Fan, S.; Wang, J.; Yan, Y.; Wang, J.; Jia, Y. Excellent Degradation Performance of a Versatile Phthalic Acid Esters-Degrading Bacterium and Catalytic Mechanism of Monoalkyl Phthalate Hydrolase. Int. J. Mol. Sci. 2018, 19, 2803. https://doi.org/10.3390/ijms19092803
Fan S, Wang J, Yan Y, Wang J, Jia Y. Excellent Degradation Performance of a Versatile Phthalic Acid Esters-Degrading Bacterium and Catalytic Mechanism of Monoalkyl Phthalate Hydrolase. International Journal of Molecular Sciences. 2018; 19(9):2803. https://doi.org/10.3390/ijms19092803
Chicago/Turabian StyleFan, Shuanghu, Junhuan Wang, Yanchun Yan, Jiayi Wang, and Yang Jia. 2018. "Excellent Degradation Performance of a Versatile Phthalic Acid Esters-Degrading Bacterium and Catalytic Mechanism of Monoalkyl Phthalate Hydrolase" International Journal of Molecular Sciences 19, no. 9: 2803. https://doi.org/10.3390/ijms19092803