Low Carbon Footprint Recycling of Post‐Consumer PET Plastic with a Metagenomic Polyester Hydrolase

Sonnendecker, Christian; Oeser, Juliane; Richter, P. Konstantin; Hille, Patrick; Zhao, Ziyue; Fischer, Cornelius; Lippold, Holger; Blázquez‐Sánchez, Paula; Engelberger, Felipe; Ramírez‐Sarmiento, César A.; Oeser, Thorsten; Lihanova, Yuliia; Frank, Ronny; Jahnke, Heinz‐Georg; Billig, Susan; Abel, Bernd; Sträter, Norbert; Matysik, Jörg; Zimmermann, Wolfgang

doi:10.1002/cssc.202101062

Cited by 86 publications

(139 citation statements)

References 79 publications

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“…[782][783][784] Shirke et al 785 demonstrated that the addition of glycosylation to the LCC enzyme via expression in Pichia pastoris results in greater stabilization of the enzyme, thus highlighting the potential for posttranslational modifications as another means of enzyme stabilization and engineering for industrial applicability. A similar enzyme to LCC was recently reported by Sonnendecker et al 786 that is able to achieve similarly high PET conversion with no substrate pretreatment. Additional studies to diversify the known PET hydrolytic enzyme suite will likely be enabled by computational methods and the massive number of genome and metagenome sequences that are continuously being reported.…”

Section: Biocatalysissupporting

confidence: 56%

“…Namely, it was estimated that approximately half of the energy input and GHG emissions arise from substrate pretreatment, which was modeled as thermal extrusion and cryo-grinding to yield micronized, amorphous PET. The development of enzymatic systems that can deconstruct crystalline substrates, which has been highlighted by studies as a major need for the field, 786,798,[800][801] would thus be a major step forward for this approach. Secondly, EG recovery from water was estimated to roughly equate to the other half of energy use and GHG emissions.…”

Section: Biocatalysismentioning

confidence: 99%

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Expanding Plastics Recycling Technologies: Chemical Aspects, Technology Status and Challenges

Aguirre-Villegas

Allen

et al. 2022

Preprint

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Less than 10% of the plastics generated globally are recycled, while the rest are incinerated, accumulated in landfills, or leach into the environment. New technologies are emerging to chemically recycle waste plastics that are receiving tremendous interest from academia and industry. Chemists and chemical engineers need to understand the fundamentals of these technologies to design improved systems for chemical recycling and upcycling of waste plastics. In this paper, we review the entire life cycle of plastics and options for the management of plastic waste to address barriers to industrial chemical recycling and further provide perceptions on possible opportunities with such materials. Knowledge and insights to enhance plastic recycling beyond its current scale are provided. Outstanding research problems and where researchers in the field should focus their efforts in the future are also discussed.

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Section: Biocatalysissupporting

confidence: 56%

Section: Biocatalysismentioning

confidence: 99%

Expanding Plastics Recycling Technologies: Chemical Aspects, Technology Status and Challenges

Aguirre-Villegas

Allen

et al. 2022

Preprint

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“…While this work was in progress, another crystal structure of PES-H1 (called PHL7 in the publication, PDB code: 7NEI ) was solved. 34 By soaking with various PET substrate analogues, structures of both PES-H1 and PES-H2 in complex with these ligands were obtained by us. These structures were used for exploring substrate binding modes by molecular dynamics (MD) simulations.…”

Section: Introductionmentioning

confidence: 99%

Multiple Substrate Binding Mode-Guided Engineering of a Thermophilic PET Hydrolase

Pfaff

Gao

et al. 2022

ACS Catal.

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Thermophilic polyester hydrolases (PES-H) have recently enabled biocatalytic recycling of the mass-produced synthetic polyester polyethylene terephthalate (PET), which has found widespread use in the packaging and textile industries. The growing demand for efficient PET hydrolases prompted us to solve high-resolution crystal structures of two metagenome-derived enzymes (PES-H1 and PES-H2) and notably also in complex with various PET substrate analogues. Structural analyses and computational modeling using molecular dynamics simulations provided an understanding of how product inhibition and multiple substrate binding modes influence key mechanistic steps of enzymatic PET hydrolysis. Key residues involved in substrate-binding and those identified previously as mutational hotspots in homologous enzymes were subjected to mutagenesis. At 72 °C, the L92F/Q94Y variant of PES-H1 exhibited 2.3-fold and 3.4-fold improved hydrolytic activity against amorphous PET films and pretreated real-world PET waste, respectively. The R204C/S250C variant of PES-H1 had a 6.4 °C higher melting temperature than the wild-type enzyme but retained similar hydrolytic activity. Under optimal reaction conditions, the L92F/Q94Y variant of PES-H1 hydrolyzed low-crystallinity PET materials 2.2-fold more efficiently than LCC ICCG, which was previously the most active PET hydrolase reported in the literature. This property makes the L92F/Q94Y variant of PES-H1 a good candidate for future applications in industrial plastic recycling processes.

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“…There are four thermophilic PET hydrolases that have been considered appropriate for PET biorecycling; metagenomic LCC, and variants of Cut190 and TfCut2 from actinomycetes ( Table 3 ), along with fungal HiC. More recently, two thermophilic polyesterases from metagenomic sources, namely, PHL7 ( Sonnendecker et al, 2021 ) and BhrPETase ( Xi et al, 2021 ) have emerged as promising candidates, with highly efficient activities toward amorphous PET films.…”

Section: Resultsmentioning

confidence: 99%

Identification of BgP, a Cutinase-Like Polyesterase From a Deep-Sea Sponge-Derived Actinobacterium

et al. 2022

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Many marine bacteria produce extracellular enzymes that degrade complex molecules to facilitate their growth in environmental conditions that are often harsh and low in nutrients. Marine bacteria, including those inhabiting sea sponges, have previously been reported to be a promising source of polyesterase enzymes, which have received recent attention due to their potential ability to degrade polyethylene terephthalate (PET) plastic. During the screening of 51 marine bacterial isolates for hydrolytic activities targeting ester and polyester substrates, a Brachybacterium ginsengisoli B129SM11 isolate from the deep-sea sponge Pheronema sp. was identified as a polyesterase producer. Sequence analysis of genomic DNA from strain B129SM11, coupled with a genome “mining” strategy, allowed the identification of potential polyesterases, using a custom database of enzymes that had previously been reported to hydrolyze PET or other synthetic polyesters. This resulted in the identification of a putative PET hydrolase gene, encoding a polyesterase-type enzyme which we named BgP that shared high overall similarity with three well-characterized PET hydrolases—LCC, TfCut2, and Cut190, all of which are key enzymes currently under investigation for the biological recycling of PET. In silico protein analyses and homology protein modeling offered structural and functional insights into BgP, and a detailed comparison with Cut190 revealed highly conserved features with implications for both catalysis and substrate binding. Polyesterase activity was confirmed using an agar-based polycaprolactone (PCL) clearing assay, following heterologous expression of BgP in Escherichia coli. This is the first report of a polyesterase being identified from a deep-sea sponge bacterium such as Brachybacterium ginsengisoli and provides further insights into marine-derived polyesterases, an important family of enzymes for PET plastic hydrolysis. Microorganisms living in association with sponges are likely to have increased exposure to plastics and microplastics given the wide-scale contamination of marine ecosystems with these plastics, and thus they may represent a worthwhile source of enzymes for use in new plastic waste management systems. This study adds to the growing knowledge of microbial polyesterases and endorses further exploration of marine host-associated microorganisms as a potentially valuable source of this family of enzymes for PET plastic hydrolysis.

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Low Carbon Footprint Recycling of Post‐Consumer PET Plastic with a Metagenomic Polyester Hydrolase

Cited by 86 publications

References 79 publications

Expanding Plastics Recycling Technologies: Chemical Aspects, Technology Status and Challenges

Expanding Plastics Recycling Technologies: Chemical Aspects, Technology Status and Challenges

Multiple Substrate Binding Mode-Guided Engineering of a Thermophilic PET Hydrolase

Identification of BgP, a Cutinase-Like Polyesterase From a Deep-Sea Sponge-Derived Actinobacterium

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