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• W3199524103 abstract "Plastic pollution spawned a global challenge caused by the environmental accumulation of polyethylene terephthalate (PET) plastics. Ongoing remediation efforts using microbial and engineered PET hydrolyzing enzymes (PETases) are hindered by slow depolymerization activities. Here, we report the optimized reaction conditions that leveraged the PETase hydrolase activity 2 to 3.8-fold in the presence of high NaCl concentrations. Molecular dynamics simulations (MDS) were applied to model salt-dependent conformational changes of the PETase enzyme bound to a 3-unit PET polymer. We determined that PETase interaction with flanking polymer units exhibited a striking structural disparity at low and high salt concentrations. At low salt concentrations, flanking polymer units exhibited significant bending. In contrast, at high salt concentrations, a flanking polymer unit extended, thus the catalytic triad residues S160, D206, and H237 oriented in close vicinity of the scissile ester bond of a polymer substrate. The resulting high salt-specific enzyme/substrate geometry potentially facilitated hydrolysis. We theorized that a salt-dependent conformational switch could attenuate the enzyme to a broad range of natural and artificial polymers. Altogether, new knowledge may advance the engineering of polymer hydrolase enzymes and benefit bioconversion programs." @default.
• W3199524103 created "2021-09-27" @default.
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• W3199524103 date "2021-09-23" @default.
• W3199524103 modified "2023-09-26" @default.
• W3199524103 title "Salt leverages polyethylene terephthalate hydrolase (PETase) enzymatic activity via the predicted conformational switch" @default.
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• W3199524103 doi "https://doi.org/10.1101/2021.09.23.461413" @default.
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