Work

Unveiling potential of Gordonia species and their cutinases for polyester decomposition

Year: 2025

Type: article

Abstract: ) and released 9.2 ± 0.6 μM terephthalic acid (TPA) from PET. Sequence alignment revealed three cutinases for polyester hydrolysis (Gph_Cut1, Gpa_Cut1, Gpa_Cut2) which were expressed in E. coli. The enzymes were active at pH 6 and ≥ 45 °C and retained up to 70 % of their activity after 96 h at 30 °C. The cutinases hydrolyzed PBAT, releasing up to 47.0 ± 1.5 μM TPA. In contrast, PET hydrolysis yielded soluble oligomers hydrolyzable to 57.6 ± 0.1 μM TPA using a commercial cutinase. The data show that Gordonia species could contribute to the biodegradation of PBAT in nature.

Source: International Journal of Biological Macromolecules

DOI: 10.1016/j.ijbiomac.2025.147309

Authors: Katharina Steiner, Aikaterini Xiromeriti, Nadja Lenkova, Michael Egermeier, Georg M. Guebitz, Doris Ribitsch

Institutions: Kompetenzzentrum Holz, BOKU University, Johannes Kepler University of Linz

Language: English

Topic: Enzyme Production and Characterization

Subfield: Biotechnology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Responsible consumption and production

Open Access status: hybrid

Estimated APC paid: $4,390