Biotechnological Routes for Microplastic Mitigation: Current Challenges and Future Opportunities in the Enzymatic Degradation of Synthetic Textile Waste
Abstract
1. Introduction
2. General Biodegradability Insights and Considerations
2.1. Fibre Chemistry
2.2. Molecular Orientation and Crystallinity
2.3. Presence of Finishing and Other Additives
2.4. Length and Twist of Yarns
2.5. Blended Fibres
2.6. Influence of the Fabric Structure
3. Current Scenario and Challenges
Biological Recycling
4. Future Perspectives
5. Conclusions
Author Contributions
Funding
Institutional Review Board Statement
Data Availability Statement
Acknowledgments
Conflicts of Interest
References
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| Additive | Function/Use | Substrate Applied | Impact on Biodegradability 1 | Mechanism of Impact | Reference |
|---|---|---|---|---|---|
| Plasticizers | Increase flexibility, reduce brittleness | CLF, EL, some acrylics | Negative | Increase hydrophobicity and persistence; may leach and resist microbial degradation | [38] |
| Flame retardants | Improve fire resistance | PET, PA, EL | Negative | Enhance chemical stability; reduce microbial and enzymatic accessibility | [39,40] |
| UV stabilisers | Prevent photodegradation | Outdoor PET, PA | Negative | Protect polymer chains from UV-induced breakdown, limiting degradation | [41] |
| Antioxidants | Prevents oxidative degradation during processing | All synthetic fibres | Negative | Stabilise polymer chains, reducing susceptibility to oxidative and enzymatic attack | [42,43] |
| Antimicrobial agents | Inhibit microbial growth | Sportswear, medical textiles | Negative | Suppress microbial colonisation, limiting biodegradation on initiation | [43] |
| Pigments/colorants | Provide colour and aesthetic properties | All fibres | Variable | Some are inert; others may interfere with microbial activity or leach toxic compounds | [44] |
| Nucleating agents | Promote crystallinity | PET, PLA | Negative | Increase crystalline regions, reducing enzymatic access | [45] |
| Enzyme Family | Specific Enzyme | Target Polymer/Fibre 1 | Reference |
|---|---|---|---|
| Hydrolase | PETase | PET | [65] |
| Cutinase | PET, PLA, EL | [66] | |
| Lipase | EL, PLA | [67] | |
| Esterase | PLA, EL | [68] | |
| Oxidoreductase | Laccase | PE, PP, PS | [69] |
| Peroxidase | [70] | ||
| Other enzymes | Dehalogenase | CLF | [71] |
| Carbonate hydrolase | PC | [72] | |
| Monooxygenase | Synthetic rubber | [73] |
| Substrate | Enzyme | Temperature (°C) | Time | Results | Reference |
|---|---|---|---|---|---|
| PET | PET hydrolase LCCICCG | 72 | 23 h | 31.2% degradation of the polymeric surface | [92] |
| Lipase (T. lanuginosus) | 37 | 120 h | ~7-fold increase in hydrolysis products released (with Triton X-100) vs. no detergent; lipase shows increase in dyeability (surface polar groups) in presence of plasticizer DEPA | [93] | |
| Cutinase (T. fusca) | 60 | 120 h | Increased hydrolysis rates in presence of plasticizer DEPA; improved dye ability/colour depth enhancement: ~300% for lipase, ~130% for cutinase in presence of plasticizer vs. without | [93] | |
| Cutinase (F. solani) | 37 | 120 h | Increased hydrolysis rates in presence of plasticizer DEPA; improved dye ability/colour depth enhancement: ~300% for lipase, ~130% for cutinase in presence of plasticizer vs. without | [93] | |
| Cutinase (H. insolens) | 55 | 24 h | 30 ± 2% yield of terephthalic acid (TPA) from the PET component | [94] | |
| 50 | 24 h | 97% pure terephthalic acid (TPA) | [95] | ||
| Cellulase | 55 | 24 h | 83 ± 4% yield of glucose from cotton component, without reducing the TPA yield | [94] | |
| Cutinase (T. fusca) | 60 | 120 h | Released ~50× more degradation products from amorphous than from semicrystalline fibres. | [96] | |
| Lipase (T. lanuginosus) | 37 | 120 h | Released about twice as much MHET and TA from amorphous fibres; small amounts of BHET detected only in amorphous samples | [96] | |
| Acrylic | Cutinase (F. solani) | 30 | 3 h | 30% increase in the colour depth because of more functional group available | [97] |
| Esterase (Texazym PES) | 30 | 3 h | 25% increase in the colour depth | [97] | |
| Nitrile hydratase | 20–25 | 10 min | Conversion of nitrile groups into the corresponding amides | [98] | |
| Nitrilase | 40 | 2 to 36 h | Conversion of nitrile groups into the corresponding carboxylic acids, release of ammonia and poly-acrylic acid | [99] | |
| Nitrile hydratase (C. nitrilophilus) and cutinase | 30 | 3 h | Increased surface hydrophilicity, wettability and dye-ability because of release of functional groups on the surface | [100] | |
| PA6.6 | Esterase | Room temperature | 1 h | Limited hydrolysis of the polyamide surface and release of adipic acid | [101] |
| Protease | Room temperature | 1 h | Limited hydrolysis of the polyamide surface and release of adipic acid | [101] | |
| Amidase | Room temperature | 1 h | Limited hydrolysis of the polyamide surface and release of adipic acid | [101] | |
| Cutinase (F. solani) | 37 | 4 h | Higher agitation enhanced enzymatic hydrolysis, resulting in increased amino acid release and improved dye uptake | [102] | |
| Protease (Bacillus sp.) | 35 | 4 h | Fivefold increase in amino group release as compared to cutinase; dye uptake also enhanced | [102] | |
| Protease + Lipase | 40 | 90 min | Increased release of amine groups and cleavage of peptide bonds | [103] | |
| Protease (B.licheniformis) | 60 | 1 h | Increased hydrophilicity, smoother surface of the fabric | [104] | |
| Lipase | 30 | 80 min | Enzymatic hydrolysis of PA chains and amide functional groups improved wettability and dyeability | [105] | |
| Nitrilases or nitrile hydratases/amidase (M. lutues BST20) | 60 | 24 h | Hydrolysation of the nitrile groups into the corresponding acid, release of ammonia | [106] |
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Majeed, A.; Cayuela, D.; Mijas, G.; Franchini, M.C.; Riba-Moliner, M. Biotechnological Routes for Microplastic Mitigation: Current Challenges and Future Opportunities in the Enzymatic Degradation of Synthetic Textile Waste. Polymers 2026, 18, 1419. https://doi.org/10.3390/polym18121419
Majeed A, Cayuela D, Mijas G, Franchini MC, Riba-Moliner M. Biotechnological Routes for Microplastic Mitigation: Current Challenges and Future Opportunities in the Enzymatic Degradation of Synthetic Textile Waste. Polymers. 2026; 18(12):1419. https://doi.org/10.3390/polym18121419
Chicago/Turabian StyleMajeed, Aqsa, Diana Cayuela, Gabriela Mijas, Mauro Comes Franchini, and Marta Riba-Moliner. 2026. "Biotechnological Routes for Microplastic Mitigation: Current Challenges and Future Opportunities in the Enzymatic Degradation of Synthetic Textile Waste" Polymers 18, no. 12: 1419. https://doi.org/10.3390/polym18121419
APA StyleMajeed, A., Cayuela, D., Mijas, G., Franchini, M. C., & Riba-Moliner, M. (2026). Biotechnological Routes for Microplastic Mitigation: Current Challenges and Future Opportunities in the Enzymatic Degradation of Synthetic Textile Waste. Polymers, 18(12), 1419. https://doi.org/10.3390/polym18121419

