As the demand for polyethylene terephthalate (PET) continues to rise, significant environmental pollution caused by challenges in PET degradation has garnered global attention. Given the crucial role of esterases in depolymerizing PET into reusable monomers, such enzymes capable of degrading plastics have attracted considerable interest. In this study, we used the previously reported ultra-efficient mutant of the PET-degrading enzyme Ideonella sakaiensis PETase, known as FASTase, as a positive control. We investigated the PET-degrading activity of esterase E4, derived from Altererythrobacter indicus. The results demonstrated that E4 exhibits degradative activity toward the PET substrate bis(2-hydroxyethyl) terephthalate, the PET model substrate bis(benzyloxyethyl) terephthalate, and PET nanoparticles. Notably, E4 retains its degradation activity under high-temperature and high-salt conditions and can enhance the enzymatic activity of FASTase when acting synergistically. Given the low structural and sequence similarity between E4 and IsPETase, our research broadens the scope for screening PET-degrading enzymes.
Duan et al. (Fri,) studied this question.