ArticleChem catalysis2025
Engineering PHL7 for improved poly(ethylene terephthalate) depolymerization via rational design and directed evolution.
Article in Chem catalysis, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Application of the YebF secretion pathway inRSC chemical biology · 2026Article
- A fluorescence-activated droplet sorting assay for ultra-high-throughput screening of PET hydrolases based on a pH indicator.RSC chemical biology · 2026Article
- Computational engineering of the polyester hydrolase PHL7 for efficient poly(ethylene terephthalate) degradation in biocatalytic recycling processes.Nature communications · 2026Article
- Rethinking plastic waste: innovations in enzymatic breakdown of oil-based polyesters and bioplastics.FEBS open bio · 2026Review
- Engineering a new tripartite split-ccGFP system from Corynactis californica for detecting protein-protein interactions.Scientific reports · 2025Article
- Protocol for engineering poly(ethylene terephthalate) hydrolases via directed evolution using a high-throughput screening assay.STAR protocols · 2025Article
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Authors and funding
11 authors.
Funding
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Abstract
Enzymatic depolymerization of poly(ethylene terephthalate) (PET) has emerged as a promising approach for polyester recycling, and, to date, many natural and engineered PET hydrolase enzymes have been reported. For industrial use, PET hydrolases must achieve high depolymerization extent and exhibit excellent thermostability. Here, we engineered a natural PET hydrolase, Polyester Hydrolase Leipzig #7 (PHL7), through rational design and directed evolution using a high-throughput screening platform. Four new enzymes were engineered with enhanced properties compared with the parent enzyme, wild-type PHL7 (PHL7-WT), and other benchmark PET hydrolases, under the tested conditions. In bioreactors, the exemplary engineered enzyme, PHL7-Jemez, exhibited improved ability to depolymerize amorphous PET film compared with PHL7-WT at 2.9% and 20% substrate loadings, with 37% and 270% higher hydrolysis, respectively, after 48 h. This study develops several state-of-the-art PET hydrolases and demonstrates a directed evolution platform to engineer high-performance enzymes, which can accelerate enzyme discovery toward improved biocatalytic recycling.
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