QM/MM Study of the Enzymatic Biodegradation Mechanism of Polyethylene Terephthalate
comunitat-uji-handle:10234/9
comunitat-uji-handle2:10234/160292
comunitat-uji-handle3:10234/160293
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INVESTIGACIONMetadades
Títol
QM/MM Study of the Enzymatic Biodegradation Mechanism of Polyethylene TerephthalateData de publicació
2021-06-04Editor
American Chemical SocietyISSN
1549-9596; 1549-960XCita bibliogràfica
Boneta S, Arafet K, Moliner V. QM/MM Study of the Enzymatic Biodegradation Mechanism of Polyethylene Terephthalate. J Chem Inf Model. 2021 Jun 28;61(6):3041-3051. doi: 10.1021/acs.jcim.1c00394. Epub 2021 Jun 4. PMID: 34085821.Tipus de document
info:eu-repo/semantics/articleVersió
info:eu-repo/semantics/publishedVersionParaules clau / Matèries
Resum
The environmental problems derived from the generalized plastic consumption and disposal could find a friendly solution in enzymatic biodegradation. Recently, two hydrolases from Ideonella sakaiensis 201-F6 and the ... [+]
The environmental problems derived from the generalized plastic consumption and disposal could find a friendly solution in enzymatic biodegradation. Recently, two hydrolases from Ideonella sakaiensis 201-F6 and the metagenome-derived leaf-branch compost cutinase (LCC), more specially the improved ICCG variant, have revealed degradation activity toward poly ethylene terephthalate (PET). In the present study, the reaction mechanism of this polymer breakage is studied at an atomic level by multiscale QM/MM molecular dynamics simulations, using semiempirical and DFT Hamiltonians to describe the QM region. The obtained free energy surfaces confirmed a characteristic four-step path for both systems, with activation energies in agreement with the experimental observations. Structural analysis of the evolution of the active site along the reaction progress and the study of electrostatic effects generated by the proteins reveal the similarity in the behavior of the active site of these two enzymes. The origin of the apparent better performance of the LCC-ICCG protein over PETase must be due to its capabilities of working at higher temperature and its intrinsic relationship with the crystallinity grade of the polymer. Our results may be useful for the development of more efficient enzymes in the biodegradation of PET. [-]
Publicat a
J Chem Inf Model . 2021 Jun 28;61(6):3041-3051.Entitat finançadora
Ministerio de Ciencia, Innovación y Universidades | Generalitat Valenciana | Universitat Jaume I
Codi del projecte o subvenció
PGC2018-094852-B-C21 | AICO/2019/195 | UJI-B2020-03 | APOSTD/2020/015
Drets d'accés
info:eu-repo/semantics/openAccess
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