ArticleChembiochem : a European journal of chemical biology2025
Mining Thermophile Genomes for New PETases with Exceptional Thermostabilities Using Sequence Similarity Networks.
Article in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Experimental, Genomic, and Structural Evidence Supporting Putative PET-Hydrolases in Thermophilic Bacteria Isolated From Hot Springs in Cajamarca, Peru.MicrobiologyOpen · 2026Article
- Structure-Guided Extremophile Genome Mining Expands the PETase Landscape and Reveals PET-Hydrolysing True Lipase Lineages.Microbial biotechnology · 2026Article
- Application of the YebF secretion pathway inRSC chemical biology · 2026Article
- Article
- EngineeringiScience · 2026Article
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5 authors.
Funding
Abstract
Enzymatic hydrolysis of polyethylene terephthalate (PET) is a promising technology for advancing a circular PET economy. Several PET-degrading α/β hydrolases have been identified, but the full potential of this enzyme family to catalyze PET hydrolysis remains largely unexplored. To address this, sequence similarity networks are employed to investigate the α/β hydrolase fold-5 subfamily (IPR029059) for new PETases. Priority is given to sequences from thermophiles, as thermostable enzymes are likely more suitable for industrial applications. Ten enzymes with ≈20% sequence identity to the well-known LCC-PETase are identified, and seven are successfully overexpressed and purified for in vitro characterization. Each enzyme catalyzes the hydrolysis of p-nitrophenyl butyrate, a mimic of trimeric PET, and emulsified PET nanoparticles. Notably, three enzymes are also capable of hydrolyzing PET films. Novel PETases exhibit melting temperatures (T
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