Enzymatic hydrolysis of polyethylene terephthalate films in an ultrafiltration membrane reactor

Barth, Markus; Wei, Ren; Oeser, Thorsten; Then, Johannes; Schmidt, Juliane; Wohlgemuth, Franziska; Zimmermann, Wolfgang

doi:10.1016/j.memsci.2015.07.030

Cited by 80 publications

(56 citation statements)

References 36 publications

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“…The K value of LCC was approximately 1.6‐fold lower than that of TfCut2, whereas a 1.7‐fold higher k value was obtained with LCC. The results indicate an inhibitory effect of MHET on the hydrolysis of PET films by LCC, as previously reported for TfCut2 .…”

Section: Resultssupporting

confidence: 88%

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A dual enzyme system composed of a polyester hydrolase and a carboxylesterase enhances the biocatalytic degradation of polyethylene terephthalate films

Barth

Honak

Oeser

et al. 2016

Biotechnology Journal

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180

107

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TfCut2 from Thermobifida fusca KW3 and the metagenome-derived LC-cutinase are bacterial polyester hydrolases capable of efficiently degrading polyethylene terephthalate (PET) films. Since the enzymatic PET hydrolysis is inhibited by the degradation intermediate mono-(2-hydroxyethyl) terephthalate (MHET), a dual enzyme system consisting of a polyester hydrolase and the immobilized carboxylesterase TfCa from Thermobifida fusca KW3 was employed for the hydrolysis of PET films at 60°C. HPLC analysis of the reaction products obtained after 24 h of hydrolysis showed an increased amount of soluble products with a lower proportion of MHET in the presence of the immobilized TfCa. The results indicated a continuous hydrolysis of the inhibitory MHET by the immobilized TfCa and demonstrated its advantage as a second biocatalyst in combination with a polyester hydrolase for an efficient degradation oft PET films. The dual enzyme system with LC-cutinase produced a 2.4-fold higher amount of degradation products compared to TfCut2 after a reaction time of 24 h confirming the superior activity of his polyester hydrolase against PET films.

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Section: Resultssupporting

confidence: 88%

“…The significantly higher amounts of hydrolysis product obtained with the dual enzyme reaction system containing LCC are consistent with the determined kinetic parameters of the reaction and confirm the higher PET degradation efficiency of this polyester hydrolase [10].…”

Section: Discussionsupporting

confidence: 83%

A dual enzyme system composed of a polyester hydrolase and a carboxylesterase enhances the biocatalytic degradation of polyethylene terephthalate films

Barth

Honak

Oeser

et al. 2016

Biotechnology Journal

Self Cite

180

107

View full text Add to dashboard Cite

show abstract

“…[17] Enzymatic and chemical hydrolysis of PET at neutral and alkaline condition result in a comparable composition of the soluble degradation products, from which EG can be easily recovered by distillation and TPA by filtration following its precipitation in the presence of a strong mineral acid. These values indicated the depolymerization of the PET polymers into monomers such as terephthalic acid (TPA) and ethylene glycol (EG) as well as their monoand di-esters, the release of which could be easily monitored by reversed phased high performance liquid chromatography (HPLC) and correlated with the weight loss determined with the same sample.…”

Section: Different Enzymatic Degradability Of Amorphous Pet Film and mentioning

confidence: 99%

Biocatalytic Degradation Efficiency of Postconsumer Polyethylene Terephthalate Packaging Determined by Their Polymer Microstructures

et al. 2019

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Polyethylene terephthalate (PET) is the most important mass‐produced thermoplastic polyester used as a packaging material. Recently, thermophilic polyester hydrolases such as TfCut2 from Thermobifida fusca have emerged as promising biocatalysts for an eco‐friendly PET recycling process. In this study, postconsumer PET food packaging containers are treated with TfCut2 and show weight losses of more than 50% after 96 h of incubation at 70 °C. Differential scanning calorimetry analysis indicates that the high linear degradation rates observed in the first 72 h of incubation is due to the high hydrolysis susceptibility of the mobile amorphous fraction (MAF) of PET. The physical aging process of PET occurring at 70 °C is shown to gradually convert MAF to polymer microstructures with limited accessibility to enzymatic hydrolysis. Analysis of the chain‐length distribution of degraded PET by nuclear magnetic resonance spectroscopy reveals that MAF is rapidly hydrolyzed via a combinatorial exo‐ and endo‐type degradation mechanism whereas the remaining PET microstructures are slowly degraded only by endo‐type chain scission causing no detectable weight loss. Hence, efficient thermostable biocatalysts are required to overcome the competitive physical aging process for the complete degradation of postconsumer PET materials close to the glass transition temperature of PET.

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“…), which released into the local ecosystems causing serious environmental pollution (Barth et al . 2015a). Therefore, eco‐friendly technologies need to be devised to solve this problem under the present situation of PET pollution.…”

Section: Introductionmentioning

confidence: 99%

Biodegradation of diethyl terephthalate and polyethylene terephthalate by a novel identified degraderDelftiasp. WL-3 and its proposed metabolic pathway

Liu

Dong

et al. 2018

Lett Appl Microbiol

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This study demonstrates that Delftia sp. WL-3 can mineralize completely diethyl terephthalate by biochemical processes. The study reveals the metabolic mechanism of diethyl terephthalate biodegradation. Furthermore, the cracks on the surface of Polyethylene terephthalate film that form upon inoculation with strain WL-3 were observed using SEM. These results highlight the potential of the strain WL-3 in the bioremediation of environments contaminated with Polyethylene terephthalate or diethyl terephthalate.

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Enzymatic hydrolysis of polyethylene terephthalate films in an ultrafiltration membrane reactor

Cited by 80 publications

References 36 publications

A dual enzyme system composed of a polyester hydrolase and a carboxylesterase enhances the biocatalytic degradation of polyethylene terephthalate films

A dual enzyme system composed of a polyester hydrolase and a carboxylesterase enhances the biocatalytic degradation of polyethylene terephthalate films

Biocatalytic Degradation Efficiency of Postconsumer Polyethylene Terephthalate Packaging Determined by Their Polymer Microstructures

Biodegradation of diethyl terephthalate and polyethylene terephthalate by a novel identified degraderDelftiasp. WL-3 and its proposed metabolic pathway

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