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Enzymatic Degradation of Thin Polyester Films Studied by In-situ ATR-FTIR Spectroscopy

Titelangaben

Müller, Martin ; Sudarsan, Neeraja ; Urbach, Birgit ; Gagsteiger, Andreas ; Turak, Onur ; Fery, Andreas ; Höcker, Birte:
Enzymatic Degradation of Thin Polyester Films Studied by In-situ ATR-FTIR Spectroscopy.
In: Journal of Polymers and the Environment. Bd. 34 (2026) . - 193.
ISSN 1572-8919
DOI: https://doi.org/10.1007/s10924-026-03908-1

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Angaben zu Projekten

Projekttitel:
Offizieller Projekttitel
Projekt-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
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Projektfinanzierung: Deutsche Forschungsgemeinschaft
Leibniz Research Association “Advanced Materials Safety"
BASF SE (Ludwigshafen am Rhein, Germany)

Abstract

The increasing presence of micro- and nanoplastics in the environment underscores the need for effective polymer degradation strategies and related analytics. Here we present model studies on the enzymatic degradation of polyester materials relevant for environmental protection and recycling using ATR-FTIR spectroscopy. Thin (45–59 nm) and thick (92–113 nm) poly(ethyleneterephthalate) (PET) and poly(butyleneterephthalate) (PBT) films were deposited onto silicon (Si) internal reflection elements (IRE) by spin coating or rolling from trifluoroacetic acid (TFA) solutions and annealing at 200 °C. Films were exposed to borate buffered solutions of IsPETase at 30 °C or LCC-iccg at 30 °C and 60 °C. In-situ ATR-FTIR spectroscopy was applied to monitor enzymatic degradation of the films on a molecular level complemented by ellipsometry, spectroscopic reflectometry (SR) and scanning force microscopy (SFM). Thin and thick PET and PBT films showed surface integrity in buffer at 30 °C, while only PBT and thick PET films remained stable at 60 °C. Significantly, diagnostic IR bands of PET showed decreasing intensities after contact with buffered solutions of either IsPETase at 30 °C or LCC-iccg at 30 °C and 60 °C enabling extraction of degradation amplitudes and apparent kinetic constants. Both enzymes showed different degradation kinetics: IsPETase displayed significantly higher amplitude and apparent kinetic constants of PET film degradation at 30 °C, whereas LCC-iccg at 60 °C on thick PET films exceeded even those for IsPETase at 30 °C. PBT films showed no substantial degradation except under LCC-iccg at 60 °C where a considerable polymer amount was degraded. Ellipsometry and SR data on enzymatically degraded PET and PBT film were in line with the ATR-FTIR data. SFM images of thin PET films revealed featureless granular morphologies before and a grinded texture of the silicon substrate after IsPETase treatment indicative of increased degradation, whereas, thin PBT films indicated low degradation and conserved fibrillar structures after IsPETase treatment.

Weitere Angaben

Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Keywords: enzymatic polymer degradation; PETase; polyester film; poly(ethyleneterephthalate); poly(butyleneterephthalate); in-situATR-FTIR spectroscopy
Institutionen der Universität: Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Ehemalige ProfessorInnen > Lehrstuhl Physikalische Chemie II - Univ.-Prof. Dr. Andreas Fery
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Lehrstuhl Biochemie III - Proteindesign > Lehrstuhl Biochemie III - Proteindesign - Univ.-Prof. Dr. Birte Höcker
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Lehrstuhl Biochemie III - Proteindesign
Forschungseinrichtungen > Sonderforschungsbereiche, Forschergruppen > SFB 1357 - MIKROPLASTIK
Titel an der UBT entstanden: Ja
Themengebiete aus DDC: 500 Naturwissenschaften und Mathematik > 500 Naturwissenschaften
500 Naturwissenschaften und Mathematik > 530 Physik
500 Naturwissenschaften und Mathematik > 540 Chemie
500 Naturwissenschaften und Mathematik > 550 Geowissenschaften, Geologie
500 Naturwissenschaften und Mathematik > 570 Biowissenschaften; Biologie
Eingestellt am: 30 Jul 2026 07:57
Letzte Änderung: 30 Jul 2026 07:57
URI: https://eref.uni-bayreuth.de/id/eprint/99148