<i>Is</i>PETase Is a Novel Biocatalyst for Poly(ethylene terephthalate) (PET) Hydrolysis

Kan, Yeyi; He, Libang; Luo, Yunzi; Bao, Rui

doi:10.1002/cbic.202000767

Cited by 20 publications

(19 citation statements)

References 71 publications

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“…[53][54][55][56] Similarly, acid hydrolysis processes are applied with mild reaction conditions, but with high catalyst concentrations of the mineral acids, such as H 2 SO 4 and HCl. [57][58][59][60][61][62][63] Hydrolysis is a heterogenous reaction occurring at the PET surface and is dependent upon the concentration of water and catalyst at the surfaces. 64 The relatively low activity of acid catalysts in these heterogenous reactions require long reaction times and high catalytic concentrations to achieve desired PET conversion.…”

Section: Introductionmentioning

confidence: 99%

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Aryl sulfonic acid catalysts: Effect of pendant group structure on activity in hydrolysis of polyethylene terephthalate

Abedsoltan

Coleman

2022

J of Applied Polymer Sci

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A series of aryl sulfonic acids were tested as catalysts for acid hydrolysis occurring at the surface of poly(ethylene) terephthalate (PET) particles. Specifically, p‐toluenesulfonic acid monohydrate (PTSA), 2‐naphthalenesulfonic acid (2‐NSA), and 1,5‐naphthalenedisulfonic acid tetrahydrate (1,5‐NDSA) were chosen to provide sulfonic acid active groups and varying hydrophobic functionality. The effect of catalyst concentration and reaction temperature on PET hydrolysis rate was studied. The aryl sulfonic acid catalysts exhibited much higher rates of PET hydrolysis than the mineral acid, H2SO4. At 150°C and 4 M catalyst, the time required to achieve more than 90% TPA yield was 3, 3, and 8 h, and 18 h for (PTSA), (2‐NSA), (1,5‐NDSA), and H2SO4, respectively. Ethyl acetate hydrolysis was performed as a model reaction to probe the activity of the catalysts in homogenous reactions to compare with the heterogenous hydrolysis reaction occurring at the PET surface. The higher catalytic activities for PET hydrolysis of the PTSA, 2‐NSA, and 1,5‐NDSA than H2SO4 was attributed to improved wetting by the reaction media and affinity of the aryl sulfonic acid catalysts for the PET surface.

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Section: Introductionmentioning

confidence: 99%

“…The applied catalysts are mineral bases, reported both in aqueous and non‐aqueous reaction mediums with maximum concentrations of 20 wt% 53–56 . Similarly, acid hydrolysis processes are applied with mild reaction conditions, but with high catalyst concentrations of the mineral acids, such as H 2 SO 4 and HCl 57–63 …”

Section: Introductionmentioning

confidence: 99%

Aryl sulfonic acid catalysts: Effect of pendant group structure on activity in hydrolysis of polyethylene terephthalate

Abedsoltan

Coleman

2022

J of Applied Polymer Sci

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“…IsPETase was selected because of the availability of a considerable information on its structure–function relationships and enzymatic mechanism [ 13 , 14 , 15 ]. Although IsPETase shows a lower thermal stability in comparison to homologues cutinases active on PET [ 6 ], its higher esterase activity at mild temperatures and its promiscuous specificity on other emerging polyesters (e.g., on polyethylene-2,5-furandicarboxylate) [ 16 ] render this enzyme an interesting potential candidate for several biotechnological applications [ 17 ].…”

Section: Introductionmentioning

confidence: 99%

An Efficient Protein Evolution Workflow for the Improvement of Bacterial PET Hydrolyzing Enzymes

Pirillo

Orlando

Tessaro

et al. 2021

IJMS

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Enzymatic degradation is a promising green approach to bioremediation and recycling of the polymer poly(ethylene terephthalate) (PET). In the past few years, several PET-hydrolysing enzymes (PHEs) have been discovered, and new variants have been evolved by protein engineering. Here, we report on a straightforward workflow employing semi-rational protein engineering combined to a high-throughput screening of variant libraries for their activity on PET nanoparticles. Using this approach, starting from the double variant W159H/S238F of Ideonella sakaiensis 201-F6 PETase, the W159H/F238A-ΔIsPET variant, possessing a higher hydrolytic activity on PET, was identified. This variant was stabilized by introducing two additional known substitutions (S121E and D186H) generating the TS-ΔIsPET variant. By using 0.1 mg mL−1 of TS-ΔIsPET, ~10.6 mM of degradation products were produced in 2 days from 9 mg mL−1 PET microparticles (~26% depolymerization yield). Indeed, TS-ΔIsPET allowed a massive degradation of PET nanoparticles (>80% depolymerization yield) in 1.5 h using only 20 μg of enzyme mL−1. The rationale underlying the effect on the catalytic parameters due to the F238A substitution was studied by enzymatic investigation and molecular dynamics/docking analysis. The present workflow is a well-suited protocol for the evolution of PHEs to help generate an efficient enzymatic toolbox for polyester degradation.

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“…At lower temperatures, in 2016, a novel mesophilic bacterium Ideonella sakaiensis 201-F6 was found to use PET as its main carbon and energy source [19]. A key enzyme, IsPETase (EC 3.1.1.101), was identified as being responsible for PET depolymerization, which showed more activity than others when compared at mild temperatures (27-40 • C) [19,25,26]. Several IsPETase structural studies were published [17,[27][28][29], which set the basis for mechanistic studies [30,31] as well as for the development of a series of mutants with increased activity [32] or thermostability [33][34][35][36][37].…”

Section: Introductionmentioning

confidence: 99%

Assessment of IsPETase-Assisted Depolymerization of Terephthalate Aromatic Polyesters and the Effect of the Thioredoxin Fusion Domain

et al. 2021

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Terephthalate polyesters such as poly(ethylene terephthalate) (PET) have been massively produced over the last few decades due to their attractive properties in multiple applications. However, due to their limited biodegradability, they have accumulated in landfills and oceans, posing an environmental threat. Enzymatic recycling technologies are predicted to generate long-term socioeconomic benefits. In the present work, we compared the IsPETase (from Ideonella sakaiensis 201-F6) activity on a series of polyesters, including poly(butylene) terephthalate (PBT), poly(hexamethylene) terephthalate (PHT) and Akestra™, with PET. The IsPETase showed remarkable activity toward PET (39% degradation of the original polyester) that was higher than that toward Akestra™ (0.13%), PBT (0.25%) and PHT (0.13%) after 72 h. Thus, based on experimental data and computational analysis, we report insights into IsPETase activity on a series of terephthalate-based polyesters. Aside from that, the fusion domain (Trx) effect in the production and activity of a recombinant Trx-IsPETase is reported.

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IsPETase Is a Novel Biocatalyst for Poly(ethylene terephthalate) (PET) Hydrolysis

Cited by 20 publications

References 71 publications

Aryl sulfonic acid catalysts: Effect of pendant group structure on activity in hydrolysis of polyethylene terephthalate

Aryl sulfonic acid catalysts: Effect of pendant group structure on activity in hydrolysis of polyethylene terephthalate

An Efficient Protein Evolution Workflow for the Improvement of Bacterial PET Hydrolyzing Enzymes

Assessment of IsPETase-Assisted Depolymerization of Terephthalate Aromatic Polyesters and the Effect of the Thioredoxin Fusion Domain

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