Fig. 3: Activity and thermostability measurements of discovered PETases. | Nature Communications

Fig. 3: Activity and thermostability measurements of discovered PETases.

From: Harnessing protein language model for structure-based discovery of highly efficient and robust PET hydrolases

Fig. 3

a PET film degradation activity of the previously characterized PETases compared to KbPETase. The reaction was conducted in 50 mM Glycine-NaOH (pH 9.0) at various temperatures (30, 40, 50, 55, 60 and 65 °C) for 72 h. Reactions were performed in triplicate; data are presented as mean values ± SD. b Comparison of the Tm of KbPETase with other reported WT PETases using DSF. Reactions were performed in triplicate; data are presented as mean values ± SD. c Comparison of the enzymatic kinetics curves of KbPETase, LCC and FastPETase using pNPB as the substrate. Reactions were performed in triplicate; data are presented as mean values ± SD. d The depolymerization percentages of PET by KbPETase and FastPETase at 50 °C, as well as by LCC at 65 °C, were determined through UPLC analysis of the released products. Reactions were conducted in triplicate, and the results are presented as mean values ± SD.

Back to article page