2019
DOI: 10.1101/787069
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Computational redesign of a PETase for plastic biodegradation by the GRAPE strategy

Abstract: The excessive use of plastics has been accompanied by severe ecologically damaging effects. The recent discovery of a PETase from Ideonella sakaiensis that decomposes poly(ethylene terephthalate) (PET) under mild conditions provides an attractive avenue for the biodegradation of plastics. However, the inherent instability of the enzyme limits its practical 20 15 and the Biological Resources Program (KFJ-BRP-009) of the Chinese Academy of Sciences.

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Cited by 21 publications
(47 citation statements)
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“…Moreover, Cui and coworkers developed a computational strategy for the mutational analysis of PETase and the design of a multiple mutant with enhanced thermostability when compared with the wild-type protein. This mutant designated as “duraPETase” contains the substitutions S214H-I168R-W159HS188Q-R280A-A180I-G165A-Q119Y-L117F-T140D, and it was able to degrade amorphous PET, but also longer polymers such as PBT with an optimum reaction temperature of 40 °C [ 60 ]. However, both engineered PETase mutants showed low efficiency in the degradation of crystalline high-density polymers, suggesting that the compactness of the material limits the protein access to the free chemical groups.…”
Section: Discussionmentioning
confidence: 99%
“…Moreover, Cui and coworkers developed a computational strategy for the mutational analysis of PETase and the design of a multiple mutant with enhanced thermostability when compared with the wild-type protein. This mutant designated as “duraPETase” contains the substitutions S214H-I168R-W159HS188Q-R280A-A180I-G165A-Q119Y-L117F-T140D, and it was able to degrade amorphous PET, but also longer polymers such as PBT with an optimum reaction temperature of 40 °C [ 60 ]. However, both engineered PETase mutants showed low efficiency in the degradation of crystalline high-density polymers, suggesting that the compactness of the material limits the protein access to the free chemical groups.…”
Section: Discussionmentioning
confidence: 99%
“…Engineering the formation of hydrogen bonds at the region responsible for a more stable enzyme structure is another method to gain enhanced thermostability [49]. The hydrogen bond can maintain protein higher-order structures, which can promote structural stability and improve resistance to high temperature.…”
Section: Trends Trends In In Biotechnology Biotechnologymentioning
confidence: 99%
“…For example, the formation of a water-mediated hydrogen bond between S121E and N172 residues at the highly flexible β6-β7 connecting loop region of PETase could increase the regional rigidity and lead to substantially enhanced thermostability [50]. In another study, multiple mutations including T140D, W159H, I168R, and S188Q were implemented to introduce new hydrogen bonds in PETase, and the engineered PETase had a melting temperature 31°C higher than that of the wild-type enzyme [49].…”
Section: Trends Trends In In Biotechnology Biotechnologymentioning
confidence: 99%
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“…Now the target is shifted for rational designing of thermo-stable PETase from I. sakaiensis [ 103 , 104 , 108 ]. To resolve the inherent instability problem of the PETase from Ideonalla sakaiensis at ambient temperature, its computational redesigning, and subsequent protein engineering is done to improve the enzymatic/ catalytic activity (400 fold), and durability (10 days) with higher crystallinity at 40ºC [ 109 ]. In spite of much progress, some technical barriers still hinder their direct physical application on a wider scale.…”
Section: Biotechnological Implication Of Metagenomic Informationmentioning
confidence: 99%