Computational explorations of the interaction between laccase and bisphenol A: influence of surfactant and different organic solvents

References

• J. Shen, Q. Kang, Y. Mao, M. Yuan, F. Le, X. Yang, X. Xu, and F. Jin, Urinary bisphenol A concentration is correlated with poorer oocyte retrieval and embryo implantation outcomes in patients with tubal factor infertility undergoing in vitro fertilisation, Ecotox. Environ. Safe. 187 (2020), pp. 109816.
   PubMed Web of Science ®Google Scholar
• E. Fasano and T. Cirillo, Plasticizers and bisphenol as food contaminants: Sources and human risk, Curr. Anal. Chem. 14 (2018), pp. 296–305. doi:10.2174/1573411013666170822153906.
   Web of Science ®Google Scholar
• A.M. Calafat and H.M. Koch, BPA and risk assessment, Lancet Diabetes Endocrinol. 8 (2020), pp. 269–270. doi:10.1016/S2213-8587(20)30070-X.
   PubMedGoogle Scholar
• C. Xiao, L. Wang, Q. Zhou, and X. Huang, Hazards of bisphenol A (BPA) exposure: A systematic review of plant toxicology studies, J. Hazard. Mater. 384 (2020), pp. 121488. doi:10.1016/j.jhazmat.2019.121488.
   PubMed Web of Science ®Google Scholar
• L.D. Toni, M.D.R. Ponce, G.C. Petre, K. Rtibl, A. Di Nisio, and C. Foresta, Bisphenols and male reproductive health: From toxicological models to therapeutic hypotheses, Front. Endocrinol. 11 (2020), pp. 301. doi:10.3389/fendo.2020.00301.
   PubMed Web of Science ®Google Scholar
• F. Liang, X. Huo, W. Wang, Y. Li, J. Zhang, Y. Feng, and Y. Wang, Association of bisphenol A or bisphenol S exposure with oxidative stress and immune disturbance among unexplained recurrent spontaneous abortion women, Chemosphere 257 (2020), pp. 127035. doi:10.1016/j.chemosphere.2020.127035.
   PubMed Web of Science ®Google Scholar
• J.M. Reed, P. Spinelli, S. Falcone, M. He, C.M. Goeke, and M. Susiarjo, Evaluating the effects of BPA and TBBPA exposure on pregnancy loss and maternal-fetal immune cells in mice, Environ. Health Perspect. 130 (2022), pp. 037010. doi:10.1289/EHP10640.
   PubMed Web of Science ®Google Scholar
• I. Cimmino, F. Fiory, G. Perruolo, C. Miele, F. Beguinot, P. Formisano, and F. Oriente, Potential mechanisms of bisphenol A (BPA) contributing to human disease, Int. J. Mol. Sci. 21 (2020), pp. 5761. doi:10.3390/ijms21165761.
   PubMed Web of Science ®Google Scholar
• I. Ďurovcová, S. Kyzek, J. Fabová, J. Makuková, E. Gálová, and A. Ševčovičová, Genotoxic potential of bisphenol A: A review, Environ. Pollut. 306 (2022), pp. 119346. doi:10.1016/j.envpol.2022.119346.
   PubMed Web of Science ®Google Scholar
• E.B. Simsek, B. Kilic, M. Asgin, and A. Akan, Graphene oxide based heterojunction TiO2-ZnO catalysts with outstanding photocatalytic performance for bisphenol-A, ibuprofen and flurbiprofen, J. Ind. Eng. Chem. 59 (2018), pp. 115–126. doi:10.1016/j.jiec.2017.10.014.
   Web of Science ®Google Scholar
• A. Garg, T. Singhania, A. Singh, S. Sharma, S. Rani, A. Neogy, S.R. Yadav, V.K. Sanga, and N. Garg, Photocatalytic degradation of bisphenol-A using N, Co codoped TiO2 catalyst under solar light, Sci. Rep. 9 (2019), pp. 765. doi:10.1038/s41598-018-38358-w.
   PubMed Web of Science ®Google Scholar
• C.Y. Wang, Q. Zeng, L.X. Wang, X. Fang, and G.C. Zhu, Visible-light-driven ag-doped BiOBr nanoplates with an enhanced photocatalytic performance for the degradation of bisphenol A, Nanomaterials 12 (2022), pp. 1909. doi:10.3390/nano12111909.
   Web of Science ®Google Scholar
• L.A. Goulart, S.A. Alves, and L.H. Mascaro, Photoelectrochemical degradation of bisphenol A using Cu doped WO3 electrodes, J. Electroanal. Chem. 839 (2019), pp. 123–133. doi:10.1016/j.jelechem.2019.03.027.
   Web of Science ®Google Scholar
• M.D. Simić, B.G. Savić, M.R. Ognjanović, D.M. Stanković, D.J. Relić, D.D. Aćimović, and T.P. Brdarić, Degradation of bisphenol A on SnO2-MWCNT electrode using electrochemical oxidation, J. Water Process Eng. 51 (2023), pp. 103416. doi:10.1016/j.jwpe.2022.103416.
   Web of Science ®Google Scholar
• C.G. Moreira, M.H. Moreira, V.M.O.C. Silva, H.G. Santos, D.M. Bila, and F.V. Fonseca, Treatment of bisphenol A (BPA) in water using UV/H2O2 and reverse osmosis (RO) membranes: Assessment of estrogenic activity and membrane adsorption, Water Sci. Technol. 80 (2019), pp. 2169–2178. doi:10.2166/wst.2020.024.
   PubMed Web of Science ®Google Scholar
• H. Zhang, J. Luo, and Y. Wan, Regenerable temperature-responsive biocatalytic nanofiltration membrane for organic micropollutants removal, Iscience (2022), pp. 1–21. doi:10.1016/j.isci.2021.103671.
   Web of Science ®Google Scholar
• Y. He, Y. Huang, Q. Wang, and X. Pan, Controlling waste by waste: A modified landfill leachate coagulation sludge activated peroxymonosulfate process achieves complete BPA degradation, Environ. Technol. 44 (2021), pp. 1–8. doi:10.1080/09593330.2021.1992511.
   PubMed Web of Science ®Google Scholar
• J. Bai, Y. Li, B. Song, and Q. Wang, Activation of peroxymonosulfate by modified coagulation sludge for bisphenol A degradation, Environ. Sci. Pollut. Res. 29 (2022), pp. 78832–78847. doi:10.1007/s11356-022-21419-z.
   PubMed Web of Science ®Google Scholar
• T. Garoma, S.A. Matsumoto, Y. Wu, and R. Klinger, Removal of bisphenol A and its reaction-intermediates from aqueous solution by ozonation, Ozone 32 (2010), pp. 338–343. doi:10.1080/01919512.2010.508484.
   Web of Science ®Google Scholar
• M. Bilal, T. Rasheed, F. Nabeel, H.M.N. Iqbal, and Y. Zhao, Hazardous contaminants in the environment and their laccase-assisted degradation-a review, J. Environ. Manage. 234 (2019), pp. 253–264. doi:10.1016/j.jenvman.2019.01.001.
   PubMed Web of Science ®Google Scholar
• A.M. Elsayed, M. Mahmoud, G.S.A. Abdel Karim, M. Abdelrao, and A.M. Othman, Purification and biochemical characterization of two laccase isoenzymes isolated from Trichoderma harzianum S7113 and its application for bisphenol A degradation, Microb. Cell Fact. 22 (2023), pp. 1–12. doi:10.1186/s12934-022-02011-z.
   PubMed Web of Science ®Google Scholar
• W. Zhang, K. Yin, and L. Chen, Bacteria-mediated bisphenol A degradation, Appl. Microbiol. Biot. 97 (2013), pp. 5681–5689. doi:10.1007/s00253-013-4949-z.
   PubMed Web of Science ®Google Scholar
• J. Trivedi and U. Chhaya, Bioremediation of bisphenol A found in industrial wastewater using Trametes versicolor (TV) laccase nanoemulsion-based bead organogel in packed bed reactor, Water Environ. Res. 94 (2022), pp. e10786. doi:10.1002/wer.10786.
   PubMed Web of Science ®Google Scholar
• K.H. Nguyen, V.D. Dao, T.T.H. Ngo, T.H. Nguyen, Q.T. Nguyen, and T.T. Le, Removal of bisphenol A using laccase-catalyzed electrooxidation in the presence of humic acid, Clean-Soil Air Water 50 (2022), pp. 2100368. doi:10.1002/clen.202100368.
   Web of Science ®Google Scholar
• S. Li, Q. Liu, J. Liu, K. Sun, W. Yang, Y. Si, Y. Li, and Y. Gao, Inhibition mechanisms of Fe2+/Fe3+ and Mn2+ on fungal laccase-enabled bisphenol A polyreaction, Chemosphere 307 (2022), pp. 135685. doi:10.1016/j.chemosphere.2022.135685.
   PubMed Web of Science ®Google Scholar
• R. Mehra, J. Muschiol, A.S. Meyer, and K.P. Kepp, A structural-chemical explanation of fungal laccase activity, Sci. Rep. 8 (2018), pp. 1–16. doi:10.1038/s41598-018-35633-8.
   PubMed Web of Science ®Google Scholar
• A.I. Canas and S. Camarero, Laccases and their natural mediators: Biotechnological tools for sustainable eco-friendly processes, Biotechnol. Adv. 28 (2010), pp. 694–705. doi:10.1016/j.biotechadv.2010.05.002.
   PubMed Web of Science ®Google Scholar
• T. Chairin, T. Nitheranont, A. Watanabe, Y. Asada, C. Khanongnuch, and S. Lumyong, Biodegradation of bisphenol A and decolorization of synthetic dyes by laccase from White-Rot fungus Trametes polyzona, Appl. Biochem. Biotechnol. 169 (2013), pp. 539–545. doi:10.1007/s12010-012-9990-3.
   PubMed Web of Science ®Google Scholar
• A. Sivan, New perspectives in plastic biodegradation, Curr. Opin. Biot. 22 (2011), pp. 422–426. doi:10.1016/j.copbio.2011.01.013.
   PubMed Web of Science ®Google Scholar
• W.T. Huang, R. Tai, R.S. Hseu, and C.T. Huang, Overexpression and characterization of a thermostable, pH-stable and organic solvent-tolerant Ganoderma fornicatum laccase in Pichia pastoris, Process Biochem. 46 (2011), pp. 1469–1474. doi:10.1016/j.procbio.2011.03.020.
   Web of Science ®Google Scholar
• M. Alcalde, M. Alcalde, T. Bulter, M. Zumárraga, H. García-Arellano, M. Mencía, F.J. Plou, and A. Ballesteros, Screening mutant libraries of fungal laccases in the presence of organic solvents, J. Biomol. Screen. 10 (2005), pp. 624–631. doi:10.1177/1087057105277058.
   PubMed Web of Science ®Google Scholar
• B. Rasekh, K. Khajeh, B. Ranjbar, N. Mollania, B. Almasinia, and H. Tirandaz, Protein engineering of laccase to enhance its activity and stability in the presence of organic solvents, Eng. Life Sci. 14 (2014), pp. 442–448. doi:10.1002/elsc.201300042.
   Web of Science ®Google Scholar
• R. Das, G. Li, B. Mai, and T. An, Spore cells from BPA degrading bacteria Bacillus sp. GZB displaying high laccase activity and stability for BPA degradation, Sci. Total Environ. 640 (2018), pp. 798–806. doi:10.1016/j.scitotenv.2018.05.379.
   PubMed Web of Science ®Google Scholar
• K. Piontek, M. Antorini, and T. Choinowski, Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-Å resolution containing a full complement of coppers, J. Biol. Chem. 277 (2002), pp. 37663–37669. doi:10.1074/jbc.M204571200.
   PubMed Web of Science ®Google Scholar
• M.H. Wu, C.C. Lee, A.S. Hsiao, S.M. Yu, A.H.J. Wang, and T.H.D. Ho, Kinetic analysis and structural studies of a high‐efficiency laccase from Cerrena sp. RSD 1, FEBS Open Bio. 8 (2018), pp. 1230–1246. doi:10.1002/2211-5463.12459.
   PubMed Web of Science ®Google Scholar
• J. Rodakiewicz-Nowak and A. Jarosz-Wilkołazka, Catalytic activity of Cerrena unicolor laccase in aqueous solutions of water-miscible organic solvents-experimental and numerical description, J. Mol. Catal. B-Enzym. 44 (2007), pp. 53–59. doi:10.1016/j.molcatb.2006.08.005.
   Web of Science ®Google Scholar
• J. Zakzeski, A.L. Jongerius, P.C.A. Bruijnincx, and B.M. Weckhuysen, Catalytic lignin valorization process for the production of aromatic chemicals and hydrogen, ChemSuschem 5 (2012), pp. 1602–1609. doi:10.1002/cssc.201100699.
   PubMed Web of Science ®Google Scholar
• J. Tominaga, J. Michizoe, N. Kamiya, H. Ichinose, T. Maruyama, and M. Goto, Factors affecting the oxidative activity of laccase towards biphenyl derivatives in homogeneous aqueous-organic systems, J. Biosci. Bioeng. 98 (2004), pp. 14–19. doi:10.1016/S1389-1723(04)70236-4.
   PubMed Web of Science ®Google Scholar
• M.H. Wu, M.C. Lin, C.C. Lee, S.M. Yu, A.H.J. Wang, and T.H.D. Ho, Enhancement of laccase activity by pre-incubation with organic solvents, Sci. Rep. 9 (2019), pp. 9754. doi:10.1038/s41598-019-45118-x.
   PubMed Web of Science ®Google Scholar
• Y. Liu, Z. Liu, G. Zeng, M. Chen, Y. Jiang, B. Shao, and Y. Liu, Effect of surfactants on the interaction of phenol with laccase: Molecular docking and molecular dynamics simulation studies, J. Hazard. Mater. 357 (2018), pp. 10–18. doi:10.1016/j.jhazmat.2018.05.042.
   PubMed Web of Science ®Google Scholar
• L. Chen, X. Huang, Y.F. Li, B. Zhao, M. Liang, and R.G. Wang, Structural and energetic basis of interaction between human estrogen-related receptor γ and environmental endocrine disruptors from multiple molecular dynamics simulations and free energy predictions, J. Hazard. Mater. 443 (2023), pp. 130174. doi:10.1016/j.jhazmat.2022.130174.
   PubMed Web of Science ®Google Scholar
• P. Bhatt, K. Bhatt, W.J. Chen, Y. Huang, Y. Xiao, S. Wu, and S. Chen, Bioremediation potential of laccase for catalysis of glyphosate, isoproturon, lignin, and parathion: Molecular docking, dynamics, and simulation, J. Hazard. Mater. 443 (2023), pp. 130319. doi:10.1016/j.jhazmat.2022.130319.
   PubMed Web of Science ®Google Scholar
• R. Dennington, T.A. Keith, and J.M. Millam, GaussView, Version 5.0, Semichem Inc., Shawnee Mission, KS, 2016; software available at http://gaussian.com/citation/.
   Google Scholar
• D.S. Goodsell and A.J. Olson, AutoDock; software available at https://autodock.scripps.edu/.
   Google Scholar
• A.K. Malde, L. Zuo, M. Breeze, M. Stroet, D. Poger, P.C. Nair, C. Oostenbrink, and A.E. Mark, An automated force field topology builder (ATB) and repository: Version 1.0, J. Chem. Theory Comput. 7 (2011), pp. 4026–4037. doi:10.1021/ct200196m.
   PubMed Web of Science ®Google Scholar
• H.J.C. Berendsen, J.P.M. Postma, W.F.V. Gunsteren, and J. Hermans, Interaction models for water in relation to protein hydration. Intermolecular Forces: Proceedings of the Fourteenth Jerusalem Symposium on Quantum Chemistry and Biochemistry Held in Jerusalem, Israel, 1981, pp. 331–342.
   Google Scholar
• G. Bussi, D. Donadio, and M. Parrinello, Canonical sampling through velocity rescaling, J. Chem. Phys. 126 (2007), pp. 1–8. doi:10.1063/1.2408420.
   Web of Science ®Google Scholar
• H.J.C. Berendsen, J.P.M. Postma, W.F. van Gunsteren, A. DiNola, and J.R. Haak, Molecular dynamics with coupling to an external bath, J. Chem. Phys. 81 (1984), pp. 3684–3690. doi:10.1063/1.448118.
   Web of Science ®Google Scholar
• S. Pronk, S. Páll, and R. Schulz, GROMACS 4.5: A high-throughput and highly parallel open source molecular simulation toolkit, Bioinformatics 29 (2013), pp. 845–854. doi:10.1093/bioinformatics/btt055.
   PubMed Web of Science ®Google Scholar
• D. Van Der Spoel, E. Lindahl, B. Hess, G. Groenhof, A.E. Mark, and H.J.C. Berendsen, GROMACS: Fast, flexible, and free, J. Comput. Chem. 26 (2005), pp. 1701–1718. doi:10.1002/jcc.20291.
   PubMed Web of Science ®Google Scholar
• N. Schmid, A.P. Eichenberger, A. Choutko, S. Riniker, M. Winger, A.E. Mark, and W.F. van Gunsteren, Definition and testing of the GROMOS force-field versions 54A7 and 54B7, Eur. Biophys. J. 40 (2011), pp. 843–856. doi:10.1007/s00249-011-0700-9.
   PubMed Web of Science ®Google Scholar
• T. Darden, D. York, and L. Pedersen, Particle mesh Ewald: An N. log (N) method for Ewald sums in large systems, J. Chem. Phys. 98 (1993), pp. 10089–10092. doi:10.1063/1.464397.
   Web of Science ®Google Scholar
• R. Kumari and R. Kumar, G_mmpbsa-A GROMACS tool for high-throughput MM-PBSA calculations, J. Chem. Inf. Model. 54 (2014), pp. 1951–1962. doi:10.1021/ci500020m.
   PubMed Web of Science ®Google Scholar
• N.A. Baker, D. Sept, S. Joseph, M.J. Holst, and J.A. McCammon, Electrostatics of nanosystems: Application to microtubules and the ribosome, Proc. Natl. Acad. Sci. USA 98 (2001), pp. 10037–10041. doi:10.1073/pnas.181342398.
   PubMed Web of Science ®Google Scholar
• J.M. Swanson, R.H. Henchman, and J.A. McCammon, Revisiting free energy calculations: A theoretical connection to MM/PBSA and direct calculation of the association free energy, Biophys. J. 86 (2004), pp. 67–74. doi:10.1016/S0006-3495(04)74084-9.
   PubMed Web of Science ®Google Scholar
• T. Hou, J. Wang, Y. Wang, and W. Li, Assessing the performance of the MM/PBSA and MM/GBSA methods. 1. The accuracy of binding free energy calculations based on molecular dynamics simulations, J. Chem. Inf. Model. 51 (2011), pp. 69–82. doi:10.1021/ci100275a.
   PubMed Web of Science ®Google Scholar
• D. Sitkoff, K.A. Sharp, and B. Honig, Accurate calculation of hydration free energies using macroscopic solvent models, J. Phys. Chem. 98 (1994), pp. 1978–1988. doi:10.1021/j100058a043.
   Web of Science ®Google Scholar
• H. Sun, Y. Li, M. Shen, S. Tian, L. Xu, P. Pan, Y. Guan, and T. Hou, Assessing the performance of MM/PBSA and MM/GBSA methods. 5. Improved docking performance using high solute dielectric constant MM/GBSA and MM/PBSA rescoring, Phys. Chem. Chem. Phys. 16 (2014), pp. 22035–22045. doi:10.1039/C4CP03179B.
   PubMed Web of Science ®Google Scholar
• Y.F. Li, L. Chen, Y. Sun, R.G. Wang, B. Zhao, and T. Jing, Exploring the effect of surfactants on the interaction between laccase and bisphenol A by molecular docking, molecular dynamics, and energy calculation, J. Mol. Liq. 382 (2023), pp. 121928. doi:10.1016/j.molliq.2023.121928.
   Web of Science ®Google Scholar
• J. Bergfreund, S. Siegenthaler, V. Lutz-Bueno, P. Bertsch, and P. Fischer, Surfactant adsorption to different fluid interfaces, Langmuir 37 (2021), pp. 6722–6727. doi:10.1021/acs.langmuir.1c00668.
   PubMed Web of Science ®Google Scholar
• C. Reichardt and T. Welton, Solvents and Solvent Effects in Organic Chemistry, John Wiley & Sons, Washington, 2011.
   Google Scholar
• A.L. Serdakowski and J.S. Dordick, Enzyme activation for organic solvents made easy, Trends Biot. 26 (2008), pp. 48–54. doi:10.1016/j.tibtech.2007.10.007.
   PubMed Web of Science ®Google Scholar