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This highly environment friendly, optimized enzyme outperforms all PET hydrolases reported to date, together with an enzyme8,9 from the bacterium Ideonella sakaiensis pressure 201-F6 (even assisted by a secondary enzyme10) and related improved variants11,12,13,14 that have attracted latest curiosity. We also present that biologically recycled PET exhibiting the identical properties as petrochemical PET might be produced from enzymatically depolymerized PET waste, earlier than being processed into bottles, thereby contributing towards the concept of a circular pet plastic containers financial system. Open Access articles citing this text. The authors declare that every one knowledge supporting the findings of this research are available within the article, its Extended Data, its Source Data or from the corresponding authors upon cheap request. The atomic coordinates and structure components of the reported structures have been deposited in the Protein Data Bank beneath accession codes 6THS for LCC-S165A and 6THT for ICCG-S165A. PlasticsEurope. Plastics-the facts 2019. An evaluation of European plastics manufacturing, demand and waste knowledge.
Minibio reactors. M.D. characterized PET powders. E.G., M.D., M. Chateau and M. Cot developed the scheme for purifying terephthalic acid and supervised the production of PET and bottles. M. Chateau, A.M., I.A., V.T. S.D. wrote the original draft. All authors reviewed and accepted the manuscript. Correspondence to I. André, S. Duquesne or A. Marty. E.G., M.D., M. Chateau and A.M. Carbios. V.T. has been an worker of Carbios since January 2019. C.M.T., H.T., V.T., M.-L.D., S.D., I.A., S.B. A.M. have filed patents WO 2018/011284 and WO 2018/011281 for ‘Novel esterases and uses thereof’. H.T., M.-L.D., S.D., A.M., M.D. M. Chateau have filed patent WO 2017/198786, ‘A process for degrading plastic products’, for protection of part of the work described herein. Confidentiality agreements stop them from disclosing any newly submitted declaration of invention. All other authors declare no competing interests. Peer evaluation data Nature thanks Peter Rem and the other, nameless, reviewer(s) for his or her contribution to the peer assessment of this work.
Austin, H. P. et al. Characterization and engineering of a plastic-degrading aromatic polyesterase. Proc. Natl Acad. Sci. Taniguchi, I. et al. Biodegradation of PET: present standing and software elements. Brueckner, T., Eberl, A., Heumann, S., Rabe, M. & Guebitz, G. M. Enzymatic and chemical hydrolysis of poly (ethylene terephthalate) fabrics. Vertommen, M. A., Nierstrasz, V. A., van der Veer, M. & Warmoeskerken, M. M. Enzymatic surface modification of poly(ethylene terephthalate). Wei, R. et al. Biocatalytic degradation efficiency of postconsumer polyethylene terephthalate packaging decided by their polymer microstructures. Ronkvist, A. S. M., Xie, W., Lu, W. & Gross, R. A. Cutinase-catalyzed hydrolysis of poly(ethylene terephthalate). Zimmermann, W. & Billig, S. Enzymes for the biofunctionalization of poly(ethylene terephthalate). Adv. Biochem. Eng. Biotechnol. Kitadokoro, K. et al. Crystal construction of cutinase Est119 from Thermobifida alba AHK119 that may degrade modified polyethylene terephthalate at 1.76 Å resolution. Chen, S., Su, L., Chen, J. & Wu, J. Cutinase: characteristics, preparation, and utility.
