An engineered PET depolymerase to break down and recycle plastic bottles
Present estimates suggest that of the 359 million tons of plastics produced annually worldwide 1 , 150–200 million tons accumulate in landfill or in the natural environment 2 . Poly(ethylene terephthalate) (PET) is the most abundant polyester plastic, with almost 70 million tons manufactured annuall...
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| Published in | Nature (London) Vol. 580; no. 7802; pp. 216 - 219 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
01.04.2020
Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Present estimates suggest that of the 359 million tons of plastics produced annually worldwide
1
, 150–200 million tons accumulate in landfill or in the natural environment
2
. Poly(ethylene terephthalate) (PET) is the most abundant polyester plastic, with almost 70 million tons manufactured annually worldwide for use in textiles and packaging
3
. The main recycling process for PET, via thermomechanical means, results in a loss of mechanical properties
4
. Consequently, de novo synthesis is preferred and PET waste continues to accumulate. With a high ratio of aromatic terephthalate units—which reduce chain mobility—PET is a polyester that is extremely difficult to hydrolyse
5
. Several PET hydrolase enzymes have been reported, but show limited productivity
6
,
7
. Here we describe an improved PET hydrolase that ultimately achieves, over 10 hours, a minimum of 90 per cent PET depolymerization into monomers, with a productivity of 16.7 grams of terephthalate per litre per hour (200 grams per kilogram of PET suspension, with an enzyme concentration of 3 milligrams per gram of PET). This highly efficient, optimized enzyme outperforms all PET hydrolases reported so far, including an enzyme
8
,
9
from the bacterium
Ideonella sakaiensis
strain 201-F6 (even assisted by a secondary enzyme
10
) and related improved variants
11
–
14
that have attracted recent interest. We also show that biologically recycled PET exhibiting the same properties as petrochemical PET can be produced from enzymatically depolymerized PET waste, before being processed into bottles, thereby contributing towards the concept of a circular PET economy.
Computer-aided engineering produces improvements to an enzyme that breaks down poly(ethylene terephthalate) (PET) into its constituent monomers, which are used to synthesize PET of near-petrochemical grade that can be further processed into bottles. |
|---|---|
| AbstractList | Present estimates suggest that of the 359 million tons of plastics produced annually worldwide.sup.1, 150-200 million tons accumulate in landfill or in the natural environment.sup.2. Poly(ethylene terephthalate) (PET) is the most abundant polyester plastic, with almost 70 million tons manufactured annually worldwide for use in textiles and packaging.sup.3. The main recycling process for PET, via thermomechanical means, results in a loss of mechanical properties.sup.4. Consequently, de novo synthesis is preferred and PET waste continues to accumulate. With a high ratio of aromatic terephthalate units--which reduce chain mobility--PET is a polyester that is extremely difficult to hydrolyse.sup.5. Several PET hydrolase enzymes have been reported, but show limited productivity.sup.6,7. Here we describe an improved PET hydrolase that ultimately achieves, over 10 hours, a minimum of 90 per cent PET depolymerization into monomers, with a productivity of 16.7 grams of terephthalate per litre per hour (200 grams per kilogram of PET suspension, with an enzyme concentration of 3 milligrams per gram of PET). This highly efficient, optimized enzyme outperforms all PET hydrolases reported so far, including an enzyme.sup.8,9 from the bacterium Ideonella sakaiensis strain 201-F6 (even assisted by a secondary enzyme.sup.10) and related improved variants.sup.11-14 that have attracted recent interest. We also show that biologically recycled PET exhibiting the same properties as petrochemical PET can be produced from enzymatically depolymerized PET waste, before being processed into bottles, thereby contributing towards the concept of a circular PET economy. Present estimates suggest that of the 359 million tons of plastics produced annually worldwide(1), 150-200 million tons accumulate in landfill or in the natural environment(2). Poly(ethylene terephthalate) (PET) is the most abundant polyester plastic, with almost 70 million tons manufactured annually worldwide for use in textiles and packaging(3). The main recycling process for PET, via thermomechanical means, results in a loss of mechanical properties(4). Consequently, de novo synthesis is preferred and PET waste continues to accumulate. With a high ratio of aromatic terephthalate units-which reduce chain mobility-PET is a polyester that is extremely difficult to hydrolyse(5). Several PET hydrolase enzymes have been reported, but show limited productivity(6,7). Here we describe an improved PET hydrolase that ultimately achieves, over 10 hours, a minimum of 90 per cent PET depolymerization into monomers, with a productivity of 16.7 grams of terephthalate per litre per hour (200 grams per kilogram of PET suspension, with an enzyme concentration of 3 milligrams per gram of PET). This highly efficient, optimized enzyme outperforms all PET hydrolases reported so far, including an enzyme(8,9) from the bacterium Ideonella sakaiensis strain 201-F6 (even assisted by a secondary enzyme(10)) and related improved variants(11-14) that have attracted recent interest. We also show that biologically recycled PET exhibiting the same properties as petrochemical PET can be produced from enzymatically depolymerized PET waste, before being processed into bottles, thereby contributing towards the concept of a circular PET economy. Present estimates suggest that of the 359 million tons of plastics produced annually worldwide 1 , 150–200 million tons accumulate in landfill or in the natural environment 2 . Poly(ethylene terephthalate) (PET) is the most abundant polyester plastic, with almost 70 million tons manufactured annually worldwide for use in textiles and packaging 3 . The main recycling process for PET, via thermomechanical means, results in a loss of mechanical properties 4 . Consequently, de novo synthesis is preferred and PET waste continues to accumulate. With a high ratio of aromatic terephthalate units—which reduce chain mobility—PET is a polyester that is extremely difficult to hydrolyse 5 . Several PET hydrolase enzymes have been reported, but show limited productivity 6 , 7 . Here we describe an improved PET hydrolase that ultimately achieves, over 10 hours, a minimum of 90 per cent PET depolymerization into monomers, with a productivity of 16.7 grams of terephthalate per litre per hour (200 grams per kilogram of PET suspension, with an enzyme concentration of 3 milligrams per gram of PET). This highly efficient, optimized enzyme outperforms all PET hydrolases reported so far, including an enzyme 8 , 9 from the bacterium Ideonella sakaiensis strain 201-F6 (even assisted by a secondary enzyme 10 ) and related improved variants 11 – 14 that have attracted recent interest. We also show that biologically recycled PET exhibiting the same properties as petrochemical PET can be produced from enzymatically depolymerized PET waste, before being processed into bottles, thereby contributing towards the concept of a circular PET economy. Computer-aided engineering produces improvements to an enzyme that breaks down poly(ethylene terephthalate) (PET) into its constituent monomers, which are used to synthesize PET of near-petrochemical grade that can be further processed into bottles. Present estimates suggest that of the 359 million tons of plastics produced annually worldwide1, 150-200 million tons accumulate in landfill or in the natural environment2. Poly(ethylene terephthalate) (PET) is the most abundant polyester plastic, with almost 70 million tons manufactured annually worldwide for use in textiles and packaging3. The main recycling process for PET, via thermomechanical means, results in a loss of mechanical properties4. Consequently, de novo synthesis is preferred and PET waste continues to accumulate. With a high ratio of aromatic terephthalate units-which reduce chain mobility-PET is a polyester that is extremely difficult to hydrolyse5. Several PET hydrolase enzymes have been reported, but show limited productivity6,7. Here we describe an improved PET hydrolase that ultimately achieves, over 10 hours, a minimum of 90 per cent PET depolymerization into monomers, with a productivity of 16.7 grams of terephthalate per litre per hour (200 grams per kilogram of PET suspension, with an enzyme concentration of 3 milligrams per gram of PET). This highly efficient, optimized enzyme outperforms all PET hydrolases reported so far, including an enzyme8,9 from the bacterium Ideonella sakaiensis strain 201-F6 (even assisted by a secondary enzyme10) and related improved variants11-14 that have attracted recent interest. We also show that biologically recycled PET exhibiting the same properties as petrochemical PET can be produced from enzymatically depolymerized PET waste, before being processed into bottles, thereby contributing towards the concept of a circular PET economy.Present estimates suggest that of the 359 million tons of plastics produced annually worldwide1, 150-200 million tons accumulate in landfill or in the natural environment2. Poly(ethylene terephthalate) (PET) is the most abundant polyester plastic, with almost 70 million tons manufactured annually worldwide for use in textiles and packaging3. The main recycling process for PET, via thermomechanical means, results in a loss of mechanical properties4. Consequently, de novo synthesis is preferred and PET waste continues to accumulate. With a high ratio of aromatic terephthalate units-which reduce chain mobility-PET is a polyester that is extremely difficult to hydrolyse5. Several PET hydrolase enzymes have been reported, but show limited productivity6,7. Here we describe an improved PET hydrolase that ultimately achieves, over 10 hours, a minimum of 90 per cent PET depolymerization into monomers, with a productivity of 16.7 grams of terephthalate per litre per hour (200 grams per kilogram of PET suspension, with an enzyme concentration of 3 milligrams per gram of PET). This highly efficient, optimized enzyme outperforms all PET hydrolases reported so far, including an enzyme8,9 from the bacterium Ideonella sakaiensis strain 201-F6 (even assisted by a secondary enzyme10) and related improved variants11-14 that have attracted recent interest. We also show that biologically recycled PET exhibiting the same properties as petrochemical PET can be produced from enzymatically depolymerized PET waste, before being processed into bottles, thereby contributing towards the concept of a circular PET economy. Present estimates suggest that of the 359 million tons of plastics produced annually worldwide , 150-200 million tons accumulate in landfill or in the natural environment . Poly(ethylene terephthalate) (PET) is the most abundant polyester plastic, with almost 70 million tons manufactured annually worldwide for use in textiles and packaging . The main recycling process for PET, via thermomechanical means, results in a loss of mechanical properties . Consequently, de novo synthesis is preferred and PET waste continues to accumulate. With a high ratio of aromatic terephthalate units-which reduce chain mobility-PET is a polyester that is extremely difficult to hydrolyse . Several PET hydrolase enzymes have been reported, but show limited productivity . Here we describe an improved PET hydrolase that ultimately achieves, over 10 hours, a minimum of 90 per cent PET depolymerization into monomers, with a productivity of 16.7 grams of terephthalate per litre per hour (200 grams per kilogram of PET suspension, with an enzyme concentration of 3 milligrams per gram of PET). This highly efficient, optimized enzyme outperforms all PET hydrolases reported so far, including an enzyme from the bacterium Ideonella sakaiensis strain 201-F6 (even assisted by a secondary enzyme ) and related improved variants that have attracted recent interest. We also show that biologically recycled PET exhibiting the same properties as petrochemical PET can be produced from enzymatically depolymerized PET waste, before being processed into bottles, thereby contributing towards the concept of a circular PET economy. Present estimates suggest that ofthe 359 million tons of plastics produced annually worldwide1, 150-200 million tons accumulate in landfill or in the natural environment2. Poly(ethylene terephthalate) (PET) is the most abundant polyester plastic, with almost 70 million tons manufactured annually worldwide for use in textiles and packaging3. The main recycling process for PET, via thermomechanical means, results in a loss of mechanical properties4. Consequently, de novo synthesis is preferred and PET waste continues to accumulate. With a high ratio of aromatic terephthalate units-which reduce chain mobility-PET is a polyester that is extremely difficult to hydrolyse5. Several PET hydrolase enzymes have been reported, but show limited productivity6,7. Here we describe an improved PET hydrolase that ultimately achieves, over 10 hours, a minimum of 90 per cent PET depolymerization into monomers, with a productivity of 16.7 grams ofterephthalate per litre per hour (200 grams per kilogram of PET suspension, with an enzyme concentration of 3 milligrams per gram of PET). This highly efficient, optimized enzyme outperforms all PET hydrolases reported so far, including an enzyme8,9 from the bacterium Ideonella sakaiensis strain 201-F6 (even assisted by a secondary enzyme10) and related improved variants11-14 that have attracted recent interest. We also show that biologically recycled PET exhibiting the same properties as petrochemical PET can be produced from enzymatically depolymerized PET waste, before being processed into bottles, thereby contributing towards the concept of a circular PET economy. Present estimates suggest that of the 359 million tons of plastics produced annually worldwide.sup.1, 150-200 million tons accumulate in landfill or in the natural environment.sup.2. Poly(ethylene terephthalate) (PET) is the most abundant polyester plastic, with almost 70 million tons manufactured annually worldwide for use in textiles and packaging.sup.3. The main recycling process for PET, via thermomechanical means, results in a loss of mechanical properties.sup.4. Consequently, de novo synthesis is preferred and PET waste continues to accumulate. With a high ratio of aromatic terephthalate units--which reduce chain mobility--PET is a polyester that is extremely difficult to hydrolyse.sup.5. Several PET hydrolase enzymes have been reported, but show limited productivity.sup.6,7. Here we describe an improved PET hydrolase that ultimately achieves, over 10 hours, a minimum of 90 per cent PET depolymerization into monomers, with a productivity of 16.7 grams of terephthalate per litre per hour (200 grams per kilogram of PET suspension, with an enzyme concentration of 3 milligrams per gram of PET). This highly efficient, optimized enzyme outperforms all PET hydrolases reported so far, including an enzyme.sup.8,9 from the bacterium Ideonella sakaiensis strain 201-F6 (even assisted by a secondary enzyme.sup.10) and related improved variants.sup.11-14 that have attracted recent interest. We also show that biologically recycled PET exhibiting the same properties as petrochemical PET can be produced from enzymatically depolymerized PET waste, before being processed into bottles, thereby contributing towards the concept of a circular PET economy. Computer-aided engineering produces improvements to an enzyme that breaks down poly(ethylene terephthalate) (PET) into its constituent monomers, which are used to synthesize PET of near-petrochemical grade that can be further processed into bottles. |
| Audience | Academic |
| Author | Texier, H. Gilles, A. Folgoas, C. André, I. Topham, C. M. Desrousseaux, M.-L. Duquesne, S. Tournier, V. Moya-Leclair, E. Cioci, G. Chateau, M. David, B. Dalibey, M. Marty, A. Nomme, J. Gavalda, S. Guémard, E. Barbe, S. Kamionka, E. Cot, M. |
| Author_xml | – sequence: 1 givenname: V. surname: Tournier fullname: Tournier, V. organization: TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 2 givenname: C. M. orcidid: 0000-0002-9147-0184 surname: Topham fullname: Topham, C. M. organization: TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 3 givenname: A. surname: Gilles fullname: Gilles, A. organization: TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 4 givenname: B. surname: David fullname: David, B. organization: TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 5 givenname: C. surname: Folgoas fullname: Folgoas, C. organization: TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 6 givenname: E. surname: Moya-Leclair fullname: Moya-Leclair, E. organization: TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 7 givenname: E. surname: Kamionka fullname: Kamionka, E. organization: TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 8 givenname: M.-L. surname: Desrousseaux fullname: Desrousseaux, M.-L. organization: TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 9 givenname: H. surname: Texier fullname: Texier, H. organization: TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 10 givenname: S. surname: Gavalda fullname: Gavalda, S. organization: TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 11 givenname: M. surname: Cot fullname: Cot, M. organization: CRITT Bio-Industries, INSA – sequence: 12 givenname: E. surname: Guémard fullname: Guémard, E. organization: Carbios, Biopôle Clermont Limagne – sequence: 13 givenname: M. surname: Dalibey fullname: Dalibey, M. organization: Carbios, Biopôle Clermont Limagne – sequence: 14 givenname: J. surname: Nomme fullname: Nomme, J. organization: TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 15 givenname: G. surname: Cioci fullname: Cioci, G. organization: TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 16 givenname: S. surname: Barbe fullname: Barbe, S. organization: TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 17 givenname: M. surname: Chateau fullname: Chateau, M. organization: Carbios, Biopôle Clermont Limagne – sequence: 18 givenname: I. orcidid: 0000-0001-6280-4109 surname: André fullname: André, I. email: isabelle.andre@insa-toulouse.fr organization: TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 19 givenname: S. surname: Duquesne fullname: Duquesne, S. email: sophie.duquesne@insa-toulouse.fr organization: TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 20 givenname: A. surname: Marty fullname: Marty, A. email: alain.marty@carbios.fr organization: TBI, Université de Toulouse, CNRS, INRAE, INSA, Carbios, Biopôle Clermont Limagne |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32269349$$D View this record in MEDLINE/PubMed https://hal.inrae.fr/hal-02545880$$DView record in HAL |
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Eng.20163913314010.1007/s00449-015-1497-1 RonkvistASMXieWLuWGrossRACutinase-catalyzed hydrolysis of poly(ethylene terephthalate)Macromolecules200942512851382009MaMol..42.5128R1:CAS:528:DC%2BD1MXotVGksb0%3D10.1021/ma9005318 BruecknerTEberlAHeumannSRabeMGuebitzGMEnzymatic and chemical hydrolysis of poly (ethylene terephthalate) fabricsJ. Polym. Sci. A200846643564431:CAS:528:DC%2BD1cXht1SnsLfE10.1002/pola.22952 KitadokoroKCrystal structure of cutinase Est119 from Thermobifida alba AHK119 that can degrade modified polyethylene terephthalate at 1.76 Å resolutionPolym. Degrad. Stabil.2012977717751:CAS:528:DC%2BC38Xjt1elsrY%3D10.1016/j.polymdegradstab.2012.02.003 MartenEMüllerR-JDeckwerW-DStudies on the enzymatic hydrolysis of polyesters. II. Aliphatic-aromatic copolyestersPolym. Degrad. Stabil.2005883713811:CAS:528:DC%2BD2MXisVCks7g%3D10.1016/j.polymdegradstab.2004.12.001 Mohammad-KhahAAnsariRActivated charcoal: preparation, characterization and applications: a review articleInt. J. Chemtech Res.20141859864 R Geyer (2149_CR2) 2017; 3 T Brueckner (2149_CR15) 2008; 46 MA Vertommen (2149_CR16) 2005; 120 A Mohammad-Khah (2149_CR33) 2014; 1 K Kitadokoro (2149_CR20) 2012; 97 I Taniguchi (2149_CR14) 2019; 9 ASM Ronkvist (2149_CR18) 2009; 42 S Yoshida (2149_CR8) 2016; 351 R Wei (2149_CR17) 2019; 6 E Marten (2149_CR5) 2005; 88 S Joo (2149_CR12) 2018; 9 R Wei (2149_CR6) 2017; 10 J Then (2149_CR23) 2015; 10 W Zimmermann (2149_CR19) 2010; 125 X Han (2149_CR11) 2017; 8 S Chen (2149_CR21) 2013; 31 F Awaja (2149_CR28) 2005; 41 S Sulaiman (2149_CR25) 2014; 53 GJ Palm (2149_CR10) 2019; 10 RJ Müller (2149_CR36) 2005; 26 J Then (2149_CR26) 2016; 6 S Sulaiman (2149_CR37) 2012; 78 UT Bornscheuer (2149_CR9) 2016; 351 2149_CR1 K Ragaert (2149_CR4) 2017; 69 HP Austin (2149_CR13) 2018; 115 2149_CR34 F Kawai (2149_CR7) 2019; 103 2149_CR35 R Sowdhamini (2149_CR27) 1989; 3 R Wei (2149_CR22) 2014; 89 G Liu (2149_CR32) 2016; 39 T Kawabata (2149_CR24) 2017; 124 2149_CR3 ES Barboza Neto (2149_CR29) 2014; 17 2149_CR30 AV Gusakov (2149_CR31) 2007; 97 |
| References_xml | – reference: AustinHPCharacterization and engineering of a plastic-degrading aromatic polyesteraseProc. Natl Acad. Sci. USA2018115E4350E43571:CAS:528:DC%2BC1cXhvVGhtLnF10.1073/pnas.1718804115 – reference: SulaimanSYouDJKanayaEKogaYKanayaSCrystal structure and thermodynamic and kinetic stability of metagenome-derived LC-cutinaseBiochemistry201453185818691:CAS:528:DC%2BC2cXjsVehs7w%3D10.1021/bi401561p – reference: GusakovAVDesign of highly efficient cellulase mixtures for enzymatic hydrolysis of celluloseBiotechnol. Bioeng.200797102810381:CAS:528:DC%2BD2sXnvFahu74%3D10.1002/bit.21329 – reference: RagaertKDelvaLVan GeemKMechanical and chemical recycling of solid plastic wasteWaste Manag.20176924581:CAS:528:DC%2BC2sXhtlOhtLrO10.1016/j.wasman.2017.07.044 – reference: WeiRZimmermannWMicrobial enzymes for the recycling of recalcitrant petroleum-based plastics: how far are we?Microb. Biotechnol.201710130813221:CAS:528:DC%2BC2sXhslCntLbF10.1111/1751-7915.12710 – reference: ChenSSuLChenJWuJCutinase: characteristics, preparation, and applicationBiotechnol. Adv.201331175417671:CAS:528:DC%2BC3sXhsFGqt7vN10.1016/j.biotechadv.2013.09.005 – reference: MartenEMüllerR-JDeckwerW-DStudies on the enzymatic hydrolysis of polyesters. II. Aliphatic-aromatic copolyestersPolym. Degrad. Stabil.2005883713811:CAS:528:DC%2BD2MXisVCks7g%3D10.1016/j.polymdegradstab.2004.12.001 – reference: MüllerRJSchraderHProfeJDreslerKDeckwerW-DEnzymatic degradation of poly(ethylene terephthalate): rapid hydrolyse using a hydrolase from T. fuscaMacromol. Rapid Commun.2005261400140510.1002/marc.200500410 – reference: GeyerRJambeckJRLawKLProduction, use, and fate of all plastics ever madeSci. Adv.20173e17007822017SciA....3E0782G10.1126/sciadv.1700782 – reference: KitadokoroKCrystal structure of cutinase Est119 from Thermobifida alba AHK119 that can degrade modified polyethylene terephthalate at 1.76 Å resolutionPolym. Degrad. Stabil.2012977717751:CAS:528:DC%2BC38Xjt1elsrY%3D10.1016/j.polymdegradstab.2012.02.003 – reference: JooSStructural insight into molecular mechanism of poly(ethylene terephthalate) degradationNat. Commun.201892018NatCo...9..382J10.1038/s41467-018-02881-1 – reference: HanXStructural insight into catalytic mechanism of PET hydrolaseNat. Commun.201782017NatCo...8.2106H10.1038/s41467-017-02255-z – reference: ThenJCa2+ and Mg2+ binding site engineering increases the degradation of polyethylene terephthalate films by polyester hydrolases from Thermobifida fuscaBiotechnol. J.2015105925981:CAS:528:DC%2BC2MXhtFKgtbc%3D10.1002/biot.201400620 – reference: Mohammad-KhahAAnsariRActivated charcoal: preparation, characterization and applications: a review articleInt. J. Chemtech Res.20141859864 – reference: VertommenMANierstraszVAvan der VeerMWarmoeskerkenMMEnzymatic surface modification of poly(ethylene terephthalate)J. Biotechnol.20051203763861:CAS:528:DC%2BD2MXht1egsrrL10.1016/j.jbiotec.2005.06.015 – reference: KawabataTOdaMKawaiFMutational analysis of cutinase-like enzyme, Cut190, based on the 3D docking structure with model compounds of polyethylene terephthalateJ. Biosci. Bioeng.201712428351:CAS:528:DC%2BC2sXjtFKnurs%3D10.1016/j.jbiosc.2017.02.007 – reference: KawaiFKawabataTOdaMCurrent knowledge on enzymatic PET degradation and its possible application to waste stream management and other fieldsAppl. Microbiol. Biotechnol.2019103425342681:CAS:528:DC%2BC1MXovFakurw%3D10.1007/s00253-019-09717-y – reference: Meyer, D. H. Process for purifying terephthalic acid. US patent 3,288,849 (1966). – reference: BornscheuerUTFeeding on plasticScience2016351115411552016Sci...351.1154B1:CAS:528:DC%2BC28XksVGntL4%3D10.1126/science.aaf2853 – reference: WeiRBiocatalytic degradation efficiency of postconsumer polyethylene terephthalate packaging determined by their polymer microstructuresAdv. Sci.20196190049110.1002/advs.201900491 – reference: TaniguchiIBiodegradation of PET: current status and application aspectsACS Catal.20199408941051:CAS:528:DC%2BC1MXmslOrtr0%3D10.1021/acscatal.8b05171 – reference: Merchant Research and Consulting. Sodium sulfate: 2020 world market outlook and forecast up to 2029. https://mcgroup.co.uk/researches/sodium-sulphate (2019). – reference: RonkvistASMXieWLuWGrossRACutinase-catalyzed hydrolysis of poly(ethylene terephthalate)Macromolecules200942512851382009MaMol..42.5128R1:CAS:528:DC%2BD1MXotVGksb0%3D10.1021/ma9005318 – reference: PalmGJStructure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrateNat. Commun.2019102019NatCo..10.1717P10.1038/s41467-019-09326-3 – reference: WeiROeserTZimmermannWSynthetic polyester-hydrolyzing enzymes from thermophilic actinomycetesAdv. Appl. Microbiol.20148926730510.1016/B978-0-12-800259-9.00007-X – reference: PlasticsEurope. Plastics—the facts 2019. An analysis of European plastics production, demand and waste data. PlasticsEuropehttps://www.plasticseurope.org/application/files/1115/7236/4388/FINAL_web_version_Plastics_the_facts2019_14102019.pdf (2019). – reference: BruecknerTEberlAHeumannSRabeMGuebitzGMEnzymatic and chemical hydrolysis of poly (ethylene terephthalate) fabricsJ. Polym. Sci. A200846643564431:CAS:528:DC%2BD1cXht1SnsLfE10.1002/pola.22952 – reference: LiuGZhangJBaoJCost evaluation of cellulose enzyme for industrial-scale cellulosic ethanol production based on rigorous Aspen Plus modelingBioprocess Biosyst. Eng.20163913314010.1007/s00449-015-1497-1 – reference: SulaimanSIsolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch compost by using a metagenomics approachAppl. Environ. Microbiol.201278155615621:CAS:528:DC%2BC38XjtVSntLY%3D10.1128/AEM.06725-11 – reference: Barboza NetoESCoelhoLAFForteMMCAmicoSCFerreiraCAProcessing of a LLDPE/HDPE pressure vessel liner by rotomoldingMater. Res.2014172362411:CAS:528:DC%2BC2cXptFyhur0%3D10.1590/S1516-14392013005000168 – reference: AwajaFPavelDRecycling of PETEur. Polym. J.200541145314771:CAS:528:DC%2BD2MXjslOgtbY%3D10.1016/j.eurpolymj.2005.02.005 – reference: Fullbrook, P. D. in Glucose Syrups, Science and Technology (eds Dziedzic, S. Z. & Kearsley, M. W.) 65–115 (Elsevier, 1984). – reference: PET polymer: chemical economics handbook. IHS Markit https://ihsmarkit.com/products/pet-polymer-chemical-economics-handbook.html (2018). – reference: YoshidaSA bacterium that degrades and assimilates poly(ethylene terephthalate)Science2016351119611992016Sci...351.1196Y1:CAS:528:DC%2BC28Xjs12gtr4%3D10.1126/science.aad6359 – reference: ZimmermannWBilligSEnzymes for the biofunctionalization of poly(ethylene terephthalate)Adv. Biochem. Eng. Biotechnol.201012597120 – reference: ThenJA disulfide bridge in the calcium binding site of a polyester hydrolase increases its thermal stability and activity against polyethylene terephthalateFEBS Open Bio201664254321:CAS:528:DC%2BC28Xht1Kru7rM10.1002/2211-5463.12053 – reference: SowdhaminiRStereochemical modeling of disulfide bridges. 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| Snippet | Present estimates suggest that of the 359 million tons of plastics produced annually worldwide
1
, 150–200 million tons accumulate in landfill or in the... Present estimates suggest that of the 359 million tons of plastics produced annually worldwide , 150-200 million tons accumulate in landfill or in the natural... Present estimates suggest that of the 359 million tons of plastics produced annually worldwide.sup.1, 150-200 million tons accumulate in landfill or in the... Present estimates suggest that ofthe 359 million tons of plastics produced annually worldwide1, 150-200 million tons accumulate in landfill or in the natural... Present estimates suggest that of the 359 million tons of plastics produced annually worldwide1, 150-200 million tons accumulate in landfill or in the natural... Present estimates suggest that of the 359 million tons of plastics produced annually worldwide(1), 150-200 million tons accumulate in landfill or in the... |
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| SubjectTerms | 631/45/603 631/61/338 639/638/77/603 82 Actinobacteria - enzymology Amino acids Analysis Binding sites Biotechnology Bottles Burkholderiales - enzymology Carboxylic Ester Hydrolases - chemistry Carboxylic Ester Hydrolases - metabolism Chain mobility Computer-aided design Depolymerization Disulfides - chemistry Disulfides - metabolism Enzyme Assays Enzyme Stability Enzymes Fusarium - enzymology Humanities and Social Sciences Hydrolase Hydrolases - chemistry Hydrolases - metabolism Landfills Life Sciences Materials Methods Models, Molecular Monomers multidisciplinary Mutagenesis Mutation Petrochemicals Petrochemicals industry Phthalic Acids - metabolism Plastic bottles Plastics Plastics - chemistry Plastics - metabolism Polyethylene terephthalate Polyethylene Terephthalates - chemistry Polyethylene Terephthalates - metabolism Polymerase chain reaction Polymerization Polymers Protein Engineering Recycling Science Science (multidisciplinary) Textiles Thermobifida Thermomechanical treatment Waste disposal sites Waste management |
| Title | An engineered PET depolymerase to break down and recycle plastic bottles |
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