Fig. 3
From: Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation
PETase activity of the variants. a Hydrolytic activities of IsPETase and its variants using BHET as a substrate. PETase activities of IsPETase and its variants were measured using BHET concentration of 200 mg L−1 and enzyme concentration of 50 nM. The amount of produced MHET was monitored by HPLC analysis. The PETase activities of the IsPETase variants were compared with that of the wild-type. b PETase activity of IsPETase proteins using the PET film as a substrate. PET film degradation activity of IsPETase proteins were measured using enzyme concentration of 200 nM. The amount of produced MHET and TPA was monitored by HPLC analysis. The PETase activities of the IsPETase variants were compared with that of the wild-type. The IsPETaseR280A variant showing an increased activity is highlighted with a star mark. c Electrostatic potential surface presentation of IsPETaseR280A structure. The 2-HE(MHET)4 molecule is labeled. The Arg280 residue in IsPETaseW/T and the Arg280Ala (R280A) change in IsPETaseR280A are indicated with dotted circles. Error bars represent the s.d. values obtained in duplicate experiments
