Title data
Pongratz, Annalena ; Gagsteiger, Andreas ; Höcker, Birte ; Ruckdäschel, Holger:
The Key to Enzymatic Degradation of Polybutylene Terephthalate (PBT): Influence of Semicrystalline Properties on Degradation.
In: ChemSusChem.
(24 October 2025)
.
- e202501775.
ISSN 1864-564X
DOI: https://doi.org/10.1002/cssc.202501775
Project information
| Project title: |
Project's official title Project's id SFB 1357: MIKROPLASTIK – Gesetzmäßigkeiten der Bildung, des Transports, des physikalisch-chemischen Verhaltens sowie der biologischen Effekte: Von Modell- zu komplexen Systemen als Grundlage neuer Lösungsansätze 391977956 |
|---|---|
| Project financing: |
Deutsche Forschungsgemeinschaft |
Abstract in another language
The rapidly growing plastic production and its environmental impact necessitate closed-loop recycling strategies for all polymers. For polyesters, which are susceptible to hydrolysis, enzymatic degradation offers a promising solution. While amorphous polyethylene terephthalate (PET) is already fully degradable, enzymatic breakdown of polybutylene terephthalate (PBT) remains challenging and underexplored. This study investigates the enzymatic degradability of PBT by systematically modifying its semicrystalline structure and optimizing enzymatic degradation conditions. Several PET-hydrolases were tested for their capability to degrade PBT, with LCC variants proving most effective. Increasing incubation temperatures drastically improve the release of soluble degradation products of PBT, with 80 °C as optimum. To assess the impact of semicrystalline properties, PBT substrates with varying contents of mobile amorphous fraction (MAF), rigid amorphous fraction (RAF), and crystalline fractions, as well as different lamellar morphologies, are prepared. Degradation trials reveal that lowering crystallinity significantly improve enzymatic PBT hydrolysis, yielding up to 1.7 mM of soluble products within 24 h. Both MAF and RAF are hydrolyzed at comparable rates, whereby incubation temperatures near the glass transition of RAF are required for significant hydrolysis. These findings demonstrate the interplay between material and enzyme properties, showcasing that fine-tuning both is key to advancing efficient enzymatic PBT recycling.
Further data
| Item Type: | Article in a journal |
|---|---|
| Refereed: | Yes |
| Institutions of the University: | Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry III - Protein Design > Chair Biochemistry III - Protein Design - Univ.-Prof. Dr. Birte Höcker Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry III - Protein Design Faculties > Faculty of Engineering Science > Chair Polymer Materials > Chair Polymer Materials - Univ.-Prof. Dr.-Ing. Holger Ruckdäschel Research Institutions > Collaborative Research Centers, Research Unit > SFB 1357 - MIKROPLASTIK |
| Result of work at the UBT: | Yes |
| DDC Subjects: | 500 Science > 540 Chemistry |
| Date Deposited: | 28 Oct 2025 07:16 |
| Last Modified: | 28 Oct 2025 07:16 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/95014 |

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