Computational analysis reveals temperature-induced stabilization of FAST-PETase.

ABSTRACT: More than 10 % of global solid waste consists of poly(ethyleneterephthalate) (PET). Among other techniques, PET hydrolases (PETases) can be used to depolymerize this plastic. However, wildtype PETases exhibit poor specific activities and insufficient thermostability, limiting their use in depolymerization processes which require high temperatures. In 2022, machine learning-aided enzyme engineering of a PETase stemming from the bacterium Ideonella sakaiensis (IsPETase) resulted in a more functional, active, stable, and tolerant variant (FAST-PETase). To rationalize the molecular basis of FAST-PETase's improved thermal stability, we performed comparative Constraint Network Analysis (CNAnalysis) and Molecular Dynamics (MD) simulations of wildtype IsPETase (WT-PETase) and

SUBMITTER: Stockinger P 

PROVIDER: S-EPMC11946493 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature