ArticleNature communications2023
Complete bio-degradation of poly(butylene adipate-co-terephthalate) via engineered cutinases.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
35 citing papers in PubMed, 170 citations in OpenAlex.
- Deep Learning-driven synergistic engineering of PET hydrolase for post-consumer PET depolymerization.Synthetic and systems biotechnology · 2027Article
- Recent advances in designing high-performance and enzymatically degradable plastics.Chemical science · 2026Review
- Functional dynamics and interactions within the bacterial community responsible for biodegradable plastic degradation during aerobic composting.Biodegradation · 2026Article
- Atmospheric Degradation of Pure and Rosemary (ACS omega · 2026Article
- EngineeringApplied and environmental microbiology · 2026Article
- Mechanistic insights into modulation of productive substrate accessibility for efficient PET depolymerization.Nature communications · 2026Article
- Plastic-Degrading Microorganisms: Biodegradation Pathways and Habitat Origins.Molecules (Basel, Switzerland) · 2026Review
- The Next Frontier in Biodegradable Plastics: Enzyme-Embedding Biodegradable Polymers.Biomacromolecules · 2026Review
- Structure-guided engineering of a gatekeeper residue enhances polylactic acid depolymerization by a cutinase fromFrontiers in bioengineering and biotechnology · 2026Article
- Engineered microbes to enable a circular economy for biodegradable plastics.Frontiers in microbiology · 2026Review
- Recent advances in poly(butylene adipate-Frontiers in chemistry · 2026Review
- Review
- Microplastics in human body: accumulation, natural clearance, and biomedical detoxification strategies.Biomedical engineering letters · 2025Review
- Highly efficient degradation of polybutylene succinate (PBS) and polycaprolactone (PCL) by a recombinant marine fungal cutinase.Applied and environmental microbiology · 2025Article
- Hygrothermal Degradation Behavior and Structural Evolution of Electrospun Poly(ethylene terephthalate) Fiber Mats.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Controlled Degradation of PBAT for PBAT/PLA Blend Melt-Blown Nonwovens.Macromolecular rapid communications · 2025Article
- Carnivorous plants can decompose the polyesters poly(ethylene terephthalate) and poly(butylene adipate terephthalate).Scientific reports · 2025Article
- One-Pot Depolymerization of Mixed Plastics Using a Dual Enzyme System.ChemSusChem · 2025Article
- Enzyme-Embedded Biodegradable Plastic for Sustainable Applications: Advances, Challenges, and Perspectives.ACS applied bio materials · 2025Review
- Evaluating cutinase from Fusarium oxysporum as a biocatalyst for the degradation of nine synthetic polymer.Scientific reports · 2025Article
Corrections and comments
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Authors and funding
16 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Poly(butylene adipate-co-terephthalate) (PBAT), a polyester made of terephthalic acid (TPA), 1,4-butanediol, and adipic acid, is extensively utilized in plastic production and has accumulated globally as environmental waste. Biodegradation is an attractive strategy to manage PBAT, but an effective PBAT-degrading enzyme is required. Here, we demonstrate that cutinases are highly potent enzymes that can completely decompose PBAT films in 48 h. We further show that the engineered cutinases, by applying a double mutation strategy to render a more flexible substrate-binding pocket exhibit higher decomposition rates. Notably, these variants produce TPA as a major end-product, which is beneficial feature for the future recycling economy. The crystal structures of wild type and double mutation of a cutinase from Thermobifida fusca in complex with a substrate analogue are also solved, elucidating their substrate-binding modes. These structural and biochemical analyses enable us to propose the mechanism of cutinase-mediated PBAT degradation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.