
PlasticsEurope. Plastics—the facts 2019. An analysis of European plastics production, demand and waste data. PlasticsEurope https://www.plasticseurope.org/application/files/1115/7236/4388/FINAL_web_version_Plastics_the_facts2019_14102019.pdf (2019).
Geyer, R., Jambeck, J. R. & Law, K. L. Production, use, and fate of all plastics ever made. Sci. Adv. 3, e1700782 (2017).
PET polymer: chemical economics handbook. IHS Markit https://ihsmarkit.com/products/pet-polymer-chemical-economics-handbook.html (2018).
Ragaert, K., Delva, L. & Van Geem, K. Mechanical and chemical recycling of solid plastic waste. Waste Manag. 69, 24–58 (2017).
Marten, E., Müller, R.-J. & Deckwer, W.-D. Studies on the enzymatic hydrolysis of polyesters. II. Aliphatic-aromatic copolyesters. Polym. Degrad. Stabil. 88, 371–381 (2005).
Wei, R. & Zimmermann, W. Microbial enzymes for the recycling of recalcitrant petroleum-based plastics: how far are we? Microb. Biotechnol. 10, 1308–1322 (2017).
Kawai, F., Kawabata, T. & Oda, M. Current knowledge on enzymatic PET degradation and its possible application to waste stream management and other fields. Appl. Microbiol. Biotechnol. 103, 4253–4268 (2019).
Yoshida, S. et al. A bacterium that degrades and assimilates poly(ethylene terephthalate). Science 351, 1196–1199 (2016).
Bornscheuer, U. T. Feeding on plastic. Science 351, 1154–1155 (2016).
Palm, G. J. et al. Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate. Nat. Commun. 10, 1717 (2019).
Han, X. et al. Structural insight into catalytic mechanism of PET hydrolase. Nat. Commun. 8, 2106 (2017).
Joo, S. et al. Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation. Nat. Commun. 9, 382 (2018).
Austin, H. P. et al. Characterization and engineering of a plastic-degrading aromatic polyesterase. Proc. Natl Acad. Sci. USA 115, E4350–E4357 (2018).
Taniguchi, I. et al. Biodegradation of PET: current status and application aspects. ACS Catal. 9, 4089–4105 (2019).
Brueckner, T., Eberl, A., Heumann, S., Rabe, M. & Guebitz, G. M. Enzymatic and chemical hydrolysis of poly (ethylene terephthalate) fabrics. J. Polym. Sci. A 46, 6435–6443 (2008).
Vertommen, M. A., Nierstrasz, V. A., van der Veer, M. & Warmoeskerken, M. M. Enzymatic surface modification of poly(ethylene terephthalate). J. Biotechnol. 120, 376–386 (2005).
Wei, R. et al. Biocatalytic degradation efficiency of postconsumer polyethylene terephthalate packaging determined by their polymer microstructures. Adv. Sci. 6, 1900491 (2019).
Ronkvist, A. S. M., Xie, W., Lu, W. & Gross, R. A. Cutinase-catalyzed hydrolysis of poly(ethylene terephthalate). Macromolecules 42, 5128–5138 (2009).
Zimmermann, W. & Billig, S. Enzymes for the biofunctionalization of poly(ethylene terephthalate). Adv. Biochem. Eng. Biotechnol. 125, 97–120 (2010).
Kitadokoro, K. et al. Crystal structure of cutinase Est119 from Thermobifida alba AHK119 that can degrade modified polyethylene terephthalate at 1.76 Å resolution. Polym. Degrad. Stabil. 97, 771–775 (2012).
Chen, S., Su, L., Chen, J. & Wu, J. Cutinase: characteristics, preparation, and application. Biotechnol. Adv. 31, 1754–1767 (2013).
Wei, R., Oeser, T. & Zimmermann, W. Synthetic polyester-hydrolyzing enzymes from thermophilic actinomycetes. Adv. Appl. Microbiol. 89, 267–305 (2014).
Then, J. et al. Ca2+ and Mg2+ binding site engineering increases the degradation of polyethylene terephthalate films by polyester hydrolases from Thermobifida fusca. Biotechnol. J. 10, 592–598 (2015).
Kawabata, T., Oda, M. & Kawai, F. Mutational analysis of cutinase-like enzyme, Cut190, based on the 3D docking structure with model compounds of polyethylene terephthalate. J. Biosci. Bioeng. 124, 28–35 (2017).
Sulaiman, S., You, D. J., Kanaya, E., Koga, Y. & Kanaya, S. Crystal structure and thermodynamic and kinetic stability of metagenome-derived LC-cutinase. Biochemistry 53, 1858–1869 (2014).
Then, J. et al. A disulfide bridge in the calcium binding site of a polyester hydrolase increases its thermal stability and activity against polyethylene terephthalate. FEBS Open Bio 6, 425–432 (2016).
Sowdhamini, R. et al. Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis. Protein Eng. 3, 95–103 (1989).
Awaja, F. & Pavel, D. Recycling of PET. Eur. Polym. J. 41, 1453–1477 (2005).
Barboza Neto, E. S., Coelho, L. A. F., Forte, M. M. C., Amico, S. C. & Ferreira, C. A. Processing of a LLDPE/HDPE pressure vessel liner by rotomolding. Mater. Res. 17, 236–241 (2014).
Fullbrook, P. D. in Glucose Syrups, Science and Technology (eds Dziedzic, S. Z. & Kearsley, M. W.) 65–115 (Elsevier, 1984).
Gusakov, A. V. et al. Design of highly efficient cellulase mixtures for enzymatic hydrolysis of cellulose. Biotechnol. Bioeng. 97, 1028–1038 (2007).
Liu, G., Zhang, J. & Bao, J. Cost evaluation of cellulose enzyme for industrial-scale cellulosic ethanol production based on rigorous Aspen Plus modeling. Bioprocess Biosyst. Eng. 39, 133–140 (2016).
Mohammad-Khah, A. & Ansari, R. Activated charcoal: preparation, characterization and applications: a review article. Int. J. Chemtech Res. 1, 859–864 (2014).
Meyer, D. H. Process for purifying terephthalic acid. US patent 3,288,849 (1966).
Merchant Research and Consulting. Sodium sulfate: 2020 world market outlook and forecast up to 2029. https://mcgroup.co.uk/researches/sodium-sulphate (2019).
Müller, R. J., Schrader, H., Profe, J., Dresler, K. & Deckwer, W.-D. Enzymatic degradation of poly(ethylene terephthalate): rapid hydrolyse using a hydrolase from T. fusca. Macromol. Rapid Commun. 26, 1400–1405 (2005).
Sulaiman, S. et al. Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch compost by using a metagenomics approach. Appl. Environ. Microbiol. 78, 1556–1562 (2012).