Improving the Catalytic Activity and Thermostability of FAST-PETase with a Multifunctional Short Peptide.

ABSTRACT: Previous reports indicated that self-assembling amphipathic peptide S1v1 (AEAEAHAH)₂ significantly enhances the soluble expression, thermostability, and activity of the target proteins when fused to them. In order to obtain high-efficiency enzymes for the large-scale degradation of polyethylene terephthalate (PET), this multifunctional peptide was fused to the N- and C-terminus of FAST-PETase, a variant of Ideonella sakaiensis PETase (IsPETase), with a PT-linker (TTVTTPQTS) harbored between the target protein and the multifunctional peptide. Consistent with previous reports, S1v1 increased the solubility of FAST-PETase slightly. Moreover, it increased the activity of FAST-PETase dramatically. The amount of terephthalic acid (TPA) and mono(2-hydroxyethyl) terephthal

SUBMITTER: Yang J 

PROVIDER: S-EPMC12190498 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature