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      Biocatalysis as a green route for recycling the recalcitrant plastic polyethylene terephthalate

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      Author(s): 1 , , 1 ,
      Publication date (Electronic):
      Journal: Microbial Biotechnology
      Publisher: John Wiley and Sons Inc.

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          Abstract

          Biocatalysis can enable a closed‐loop recycling of post‐consumer PET waste.

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          Microbial enzymes for the recycling of recalcitrant petroleum‐based plastics: how far are we?

          Ren Wei, Wolfgang Zimmermann (2017)
          Summary Petroleum‐based plastics have replaced many natural materials in their former applications. With their excellent properties, they have found widespread uses in almost every area of human life. However, the high recalcitrance of many synthetic plastics results in their long persistence in the environment, and the growing amount of plastic waste ending up in landfills and in the oceans has become a global concern. In recent years, a number of microbial enzymes capable of modifying or degrading recalcitrant synthetic polymers have been identified. They are emerging as candidates for the development of biocatalytic plastic recycling processes, by which valuable raw materials can be recovered in an environmentally sustainable way. This review is focused on microbial biocatalysts involved in the degradation of the synthetic plastics polyethylene, polystyrene, polyurethane and polyethylene terephthalate (PET). Recent progress in the application of polyester hydrolases for the recovery of PET building blocks and challenges for the application of these enzymes in alternative plastic waste recycling processes will be discussed.
          Article 0 comments Cited 197 times – based on 0 reviews     Review now
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            Isolation of a novel cutinase homolog with polyethylene terephthalate-degrading activity from leaf-branch compost by using a metagenomic approach.

            Sintawee Sulaiman, Saya Yamato, Eiko Kanaya … (2012)
            The gene encoding a cutinase homolog, LC-cutinase, was cloned from a fosmid library of a leaf-branch compost metagenome by functional screening using tributyrin agar plates. LC-cutinase shows the highest amino acid sequence identity of 59.7% to Thermomonospora curvata lipase. It also shows the 57.4% identity to Thermobifida fusca cutinase. When LC-cutinase without a putative signal peptide was secreted to the periplasm of Escherichia coli cells with the assistance of the pelB leader sequence, more than 50% of the recombinant protein, termed LC-cutinase*, was excreted into the extracellular medium. It was purified and characterized. LC-cutinase* hydrolyzed various fatty acid monoesters with acyl chain lengths of 2 to 18, with a preference for short-chain substrates (C(4) substrate at most) most optimally at pH 8.5 and 50°C, but could not hydrolyze olive oil. It lost activity with half-lives of 40 min at 70°C and 7 min at 80°C. LC-cutinase* had an ability to degrade poly(ε-caprolactone) and polyethylene terephthalate (PET). The specific PET-degrading activity of LC-cutinase* was determined to be 12 mg/h/mg of enzyme (2.7 mg/h/μkat of pNP-butyrate-degrading activity) at pH 8.0 and 50°C. This activity is higher than those of the bacterial and fungal cutinases reported thus far, suggesting that LC-cutinase* not only serves as a good model for understanding the molecular mechanism of PET-degrading enzyme but also is potentially applicable for surface modification and degradation of PET.
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              Cutinase-Catalyzed Hydrolysis of Poly(ethylene terephthalate)

              Richard Gross, Åsa Ronkvist, Wenchun Xie … (2009)
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                Author and article information

                Contributors
                Ren Wei: wei@uni-leipzig.de
                Wolfgang Zimmermann: wolfgang.zimmermann@uni-leipzig.de
                Journal
                Journal ID (nlm-ta): Microb Biotechnol
                Journal ID (iso-abbrev): Microb Biotechnol
                Journal ID (doi): 10.1111/(ISSN)1751-7915
                Journal ID (publisher-id): MBT2
                Title: Microbial Biotechnology
                Publisher: John Wiley and Sons Inc. (Hoboken )
                ISSN (Electronic): 1751-7915
                Publication date (Electronic): 12 April 2017
                Publication date Collection: November 2017
                Volume: 10
                Issue: 6 , Thematic Issue: From complex waste to plastic value ( doiID: 10.1111/mbt2.2017.10.issue-6 )
                Pages: 1302-1307
                Affiliations
                [ 1 ] Department of Microbiology and Bioprocess Technology Institute of Biochemistry Leipzig University Johannisallee 21‐23 04103 Leipzig Germany
                Author notes
                [*] [* ]For correspondence: *E‐mail wei@ 123456uni-leipzig.de ; Tel. +49‐341‐97‐36784; Fax +49‐341‐97‐36798. **E‐mail wolfgang.zimmermann@ 123456uni-leipzig.de ; Tel. +49‐341‐97‐36781; Fax 49‐341‐97‐36798.
                Article
                Publisher ID: MBT212714
                DOI: 10.1111/1751-7915.12714
                PMC ID: 5658586
                PubMed ID: 28401691
                SO-VID: 668e2439-4319-42e9-9317-163fb7d6214d
                Copyright © © 2017 The Authors. Microbial Biotechnology published by John Wiley & Sons Ltd and Society for Applied Microbiology.
                License:

                This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 29 November 2016
                Date revision received : 16 March 2017
                Date accepted : 16 March 2017
                Page count
                Figures: 1, Tables: 1, Pages: 6, Words: 4488
                Funding
                Funded by: European Union's Horizon 2020 research and innovation programme
                Award ID: 633962
                Funded by: German Federal Ministry of Education and Research
                Award ID: 031A227E
                Categories
                Subject: Opinion
                Subject: Opinion
                Custom metadata
                source-schema-version-number 2.0
                component-id mbt212714
                cover-date November 2017
                details-of-publishers-convertor Converter:WILEY_ML3GV2_TO_NLMPMC version:5.2.1 mode:remove_FC converted:27.10.2017

                ScienceOpen disciplines: Biotechnology
                Data availability:
                ScienceOpen disciplines: Biotechnology

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