Fig. 1: The discovery a PET hydrolase and initial characterizations of CaPETase.

a Maximum likelihood phylogenetic tree and percentage identity matrix of the 10 selected PETase candidate (PC1–PC10) and 17 reported PET hydrolase sequences. Bootstrap values for 1000 replications are shown at the branching edges. The colored bar represents the level of the percent identity of the enzymes, and detailed percent identity values are listed in Supplementary Fig. 31. b Protein yield and the T_m values of the 8 PCs. c PET hydrolytic activity of the eight PCs. The reaction was performed with post-consumer transparent PET powder (PC-PET^Transparent, 15 mg mL⁻¹ with 500 nM enzyme), semi-crystalline PET powder (Cry-PET, 15 mg mL⁻¹ with 2 µM enzyme), and amorphous PET film (AF-PET, 15 mg mL⁻¹ with 2 µM enzyme) in 50 mM Glycine-NaOH pH 9.0 buffer at various temperatures (30 °C, 40 °C, 50 °C, 60 °C) for 3 days. Reactions were performed in triplicate; Data are presented as mean values  ±  SD. d Comparison of the PET hydrolytic activity of CaPETase, IsPETase, LCC, and TfCut2. The reaction was conducted with Cry-PET (15 mg mL⁻¹ with 2 µM enzyme) in 50 mM Glycine-NaOH (pH 9.0) at various temperatures (30 °C, 40 °C, 50 °C, 60 °C) for 12 h. Reactions were performed in triplicate; Data are presented as mean values  ±  SD.