Engineering the catalytic activity of an Antarctic PET-degrading enzyme by loop exchange.

ABSTRACT: Several hydrolases have been described to degrade polyethylene terephthalate (PET) at moderate temperatures ranging from 25°C to 40°C. These mesophilic PET hydrolases (PETases) are less efficient in degrading this plastic polymer than their thermophilic homologs and have, therefore, been the subject of many protein engineering campaigns. However, enhancing their enzymatic activity through rational design or directed evolution poses a formidable challenge due to the need for exploring a large number of mutations. Additionally, evaluating the improvements in both activity and stability requires screening numerous variants, either individually or using high-throughput screening methods. Here, we utilize instead the design of chimeras as a protein engineering strategy to increase the activity

SUBMITTER: Blazquez-Sanchez P 

PROVIDER: S-EPMC10464292 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature