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) and released 9. 2 ± 0. 6 μM terephthalic acid (TPA) from PET. Sequence alignment revealed three cutinases for polyester hydrolysis (GphCut1, GpaCut1, GpaCut2) 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.
Steiner et al. (Tue,) studied this question.