Synergistic engineering PETase reveals loop-region mutations for enhanced catalytic activity and thermal stability.

ABSTRACT: Biodegradation of Polyethylene Terephthalate (PET) offer a strategic avenue for addressing the global plastic pollution crisis. However, the degradation performance of PET hydrolases remains a technological bottleneck for the industrial realization of plastic biodegradation. In this study, we employed an integrated strategy combining semi-rational design and directed evolution to discover new mutation sites (N114, N205, N233 and S269) that enhance the catalytic activity and thermostability of Ideonella sakaiensis PETase (IsPETase). Subsequently, through the combined design of newly discovered mutation sites, we screened the novel quadruple mutant (N114I/N205K/N233K/S269V, named QM-PETase-2), which exhibited a 4.9-fold increase in catalytic efficiency and a ΔT _m

SUBMITTER: Han Y 

PROVIDER: S-EPMC12657606 | biostudies-literature | 2026 Mar

REPOSITORIES: biostudies-literature