ArticleFrontiers in bioengineering and biotechnology2022
Molecular and Biochemical Differences of the Tandem and Cold-Adapted PET Hydrolases Ple628 and Ple629, Isolated From a Marine Microbial Consortium.
Article in Frontiers in bioengineering and biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.
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Who cites it
20 citing papers in PubMed, 1 synthesis or guideline pooled it.
- The diversity of PET degrading enzymes: A systematic review of sequence, structure, and function.Protein science : a publication of the Protein Society · 2025Pooled it
- MutexaGPT: an intuition-to-design translator for physics-based enzyme engineering.Nature computational science · 2026Article
- Computer-guided enzyme engineering of PET hydrolase mutants towards improved PET affinity.BMC biotechnology · 2026Article
- MutexaGPT: An Intuition-to-Design Translator for Physics-based Enzyme Engineering.Research square · 2026Article
- Microbial plastic degradation: enzymes, pathways, challenges, and perspectives.Microbiology and molecular biology reviews : MMBR · 2025Review
- Enhancing Cold Adaptation of Bidomain Amylases by High-Throughput Computational Engineering.Angewandte Chemie (International ed. in English) · 2025Article
- Standardization guidelines and future trends for PET hydrolase research.Nature communications · 2025Review
- One-Pot Depolymerization of Mixed Plastics Using a Dual Enzyme System.ChemSusChem · 2025Article
- Selective Modification of the Product Profile of Biocatalytic Hydrolyzed PET via Product-Specific Medium Engineering.ChemSusChem · 2025Article
- Review
- Plastic-Degrading Enzymes from Marine Microorganisms and Their Potential Value in Recycling Technologies.Marine drugs · 2024Review
- Identification and expression of MarCE, a marine carboxylesterase with synthetic ester-degrading activity.Microbial biotechnology · 2024Article
- Characterization and engineering of plastic-degrading polyesterases jmPE13 and jmPE14 fromFrontiers in bioengineering and biotechnology · 2024Article
- Comparative biodegradation analysis of three compostable polyesters by a marine microbial community.Applied and environmental microbiology · 2023Article
- Biodegradation of PET by the membrane-anchored PET esterase from the marine bacterium Rhodococcus pyridinivorans P23.Communications biology · 2023Article
- An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate.Communications chemistry · 2023Article
- Engineering the catalytic activity of an Antarctic PET-degrading enzyme by loop exchange.Protein science : a publication of the Protein Society · 2023Article
- Accelerated degradation of plastic products via yeast enzyme treatment.Scientific reports · 2023Article
- Purification and biochemical characterization of SM14est, a PET-hydrolyzing enzyme from the marine sponge-derivedFrontiers in microbiology · 2023Article
- Investigation of the halophilic PET hydrolase PET6 from Vibrio gazogenes.Protein science : a publication of the Protein Society · 2022Article
Corrections and comments
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Authors and funding
13 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Polybutylene adipate terephthalate (PBAT) is a biodegradable alternative to polyethylene and can be broadly used in various applications. These polymers can be degraded by hydrolases of terrestrial and aquatic origin. In a previous study, we identified tandem PETase-like hydrolases (Ples) from the marine microbial consortium I1 that were highly expressed when a PBAT blend was supplied as the only carbon source. In this study, the tandem Ples, Ple628 and Ple629, were recombinantly expressed and characterized. Both enzymes are mesophilic and active on a wide range of oligomers. The activities of the Ples differed greatly when model substrates, PBAT-modified polymers or PET nanoparticles were supplied. Ple629 was always more active than Ple628. Crystal structures of Ple628 and Ple629 revealed a structural similarity to other PETases and can be classified as member of the PETases IIa subclass, α/β hydrolase superfamily. Our results show that the predicted functions of Ple628 and Ple629 agree with the bioinformatic predictions, and these enzymes play a significant role in the plastic degradation by the consortium.
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