Recovery of pure PET from wool/PET/elastane textile waste through step-wise enzymatic and chemical processing

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Abstract

Textile waste is mostly incinerated because few recycling processes are available to recover valuable materials. In this work, a feasible chemo-enzymatic recycling process of wool/polyethylene terephthalate (PET)/elastane blends to recover pure PET is for the first time successfully demonstrated. Two novel enzyme formulations were selected for wool hydrolysis, whereas the recovered amino acids were quantified using high-performance liquid chromatography and two assays (Ninhydrin and Folin–Ciocalteu). Kinetic studies on the amino acid formation alongside reaction observations by scanning electron microscopy proved sufficient removal of wool within 8 hours with the new enzyme formulation, marking an acceleration compared to previous studies. Finally, elastane was separated with a non-hazardous solvent to obtain pure PET. Tensile tests on the recovered PET fibres reveal only slight changes through the enzymatic treatment and no changes induced by the applied solvent. The enzyme formulation was successfully tested on five different post-consumer wool/PET textile waste samples. This valorization approach enhances the circular economy concept for textile waste recycling.

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Most cited references 39

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An engineered PET depolymerase to break down and recycle plastic bottles

V Tournier, C M Topham, A Gilles … (2020)

Present estimates suggest that of the 359 million tons of plastics produced annually worldwide1, 150-200 million tons accumulate in landfill or in the natural environment2. Poly(ethylene terephthalate) (PET) is the most abundant polyester plastic, with almost 70 million tons manufactured annually worldwide for use in textiles and packaging3. The main recycling process for PET, via thermomechanical means, results in a loss of mechanical properties4. Consequently, de novo synthesis is preferred and PET waste continues to accumulate. With a high ratio of aromatic terephthalate units-which reduce chain mobility-PET is a polyester that is extremely difficult to hydrolyse5. Several PET hydrolase enzymes have been reported, but show limited productivity6,7. Here we describe an improved PET hydrolase that ultimately achieves, over 10 hours, a minimum of 90 per cent PET depolymerization into monomers, with a productivity of 16.7 grams of terephthalate per litre per hour (200 grams per kilogram of PET suspension, with an enzyme concentration of 3 milligrams per gram of PET). This highly efficient, optimized enzyme outperforms all PET hydrolases reported so far, including an enzyme8,9 from the bacterium Ideonella sakaiensis strain 201-F6 (even assisted by a secondary enzyme10) and related improved variants11-14 that have attracted recent interest. We also show that biologically recycled PET exhibiting the same properties as petrochemical PET can be produced from enzymatically depolymerized PET waste, before being processed into bottles, thereby contributing towards the concept of a circular PET economy.

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Microbial enzymes catalyzing keratin degradation: Classification, structure, function

Jingwen Qiu, Casper Wilkens, Kristian Barrett … (2020)

Keratin is an insoluble and protein-rich epidermal material found in e.g. feather, wool, hair. It is produced in substantial amounts as co-product from poultry processing plants and pig slaughterhouses. Keratin is packed by disulfide bonds and hydrogen bonds. Based on the secondary structure, keratin can be classified into α-keratin and β-keratin. Keratinases (EC 3.4.-.- peptide hydrolases) have major potential to degrade keratin for sustainable recycling of the protein and amino acids. Currently, the known keratinolytic enzymes belong to at least 14 different protease families: S1, S8, S9, S10, S16, M3, M4, M14, M16, M28, M32, M36, M38, M55 (MEROPS database). The various keratinolytic enzymes act via endo-attack (proteases in families S1, S8, S16, M4, M16, M36), exo-attack (proteases in families S9, S10, M14, M28, M38, M55) or by action only on oligopeptides (proteases in families M3, M32), respectively. Other enzymes, particularly disulfide reductases, also play a key role in keratin degradation as they catalyze the breakage of disulfide bonds for better keratinase catalysis. This review aims to contribute an overview of keratin biomass as an enzyme substrate and a systematic analysis of currently sequenced keratinolytic enzymes and their classification and reaction mechanisms. We also summarize and discuss keratinase assays, available keratinase structures and finally examine the available data on uses of keratinases in practical biorefinery protein upcycling applications.

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Synergistic chemo‐enzymatic hydrolysis of poly(ethylene terephthalate) from textile waste

Felice Quartinello, Simona Vajnhandl, Julija Volmajer Valh … (2017)

Summary Due to the rising global environment protection awareness, recycling strategies that comply with the circular economy principles are needed. Polyesters are among the most used materials in the textile industry; therefore, achieving a complete poly(ethylene terephthalate) (PET) hydrolysis in an environmentally friendly way is a current challenge. In this work, a chemo‐enzymatic treatment was developed to recover the PET building blocks, namely terephthalic acid (TA) and ethylene glycol. To monitor the monomer and oligomer content in solid samples, a Fourier‐transformed Raman method was successfully developed. A shift of the free carboxylic groups (1632 cm−1) of TA into the deprotonated state (1604 and 1398 cm−1) was observed and bands at 1728 and 1398 cm−1 were used to assess purity of TA after the chemo‐enzymatic PET hydrolysis. The chemical treatment, performed under neutral conditions (T = 250 °C, P = 40 bar), led to conversion of PET into 85% TA and small oligomers. The latter were hydrolysed in a second step using the Humicola insolens cutinase (HiC) yielding 97% pure TA, therefore comparable with the commercial synthesis‐grade TA (98%).

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Author and article information

Contributors

Emanuel Boschmeier: (View ORCID Profile)

Daniella Mehanni: (View ORCID Profile)

Viktor Laurin Sedlmayr: (View ORCID Profile)

Andreas Bartl: (View ORCID Profile)

Journal

Title: Waste Management & Research: The Journal for a Sustainable Circular Economy

Abbreviated Title: Waste Manag Res

Publisher: SAGE Publications

ISSN (Print): 0734-242X

ISSN (Electronic): 1096-3669

Publication date (Electronic): September 20 2024

Affiliations

[1 ]Institute of Chemical, Environmental and Bioscience Engineering, TU Wien, Vienna, Austria

[2 ]Institute of Mechanics and Mechatronics, TU Wien, Vienna, Austria

[3 ]Department of Agrobiotechnology, IFA-Tulln, Institute of Environmental Biotechnology, University of Natural Resources and Life Sciences, Tulln an der Donau, Austria

Article

DOI: 10.1177/0734242X241276089

SO-VID: 388881c2-baf3-4bab-84f8-e07fc69d73b8

License:

https://creativecommons.org/licenses/by/4.0/

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