The Esterase Gs Derived from <i>Geobacillus</i> sp. JM6 Exhibits Hydrolytic Activity on the PET Model Substrates.

ABSTRACT: The continuous increase in demand for polyethylene terephthalate (PET) has drawn global attention to the significant environmental pollution caused by the degradation of PET plastics. Exploring new PET-degrading enzymes is essential for enhancing the degradation efficiency of PET, and esterases and lipases with plastic degradation capabilities have become a focal point of research. In this study, we utilized the ultra-efficient mutant FASTase of the PET-degrading enzyme IsPETase, derived from Ideonella sakaiensis, as a positive control, based on the similarity in enzyme activity and substrate. We investigated the PET model substrate degradation activities of the esterase Gs and lipase GI, both derived from Bacillus spp., as well as the lipase CAI derived from Pseudo

SUBMITTER: Duan S 

PROVIDER: S-EPMC12562035 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature