ArticleJournal of industrial microbiology & biotechnology2017
Screening of commercial enzymes for poly(ethylene terephthalate) (PET) hydrolysis and synergy studies on different substrate sources.
Article in Journal of industrial microbiology & biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
42 citing papers in PubMed, 119 citations in OpenAlex.
- Cooperative Amidase Systems Control Product Selectivity During Enzymatic Nylon Depolymerization.Macromolecular bioscience · 2026Article
- Article
- Systematic optimization and characterization of bacterial depolymerization of poly(ethylene terephthalate) plastics.Scientific reports · 2026Article
- Inactivation of PETase at Interfaces Inhibits PET Plastic Depolymerization.ACS sustainable chemistry & engineering · 2026Article
- The Next Frontier in Biodegradable Plastics: Enzyme-Embedding Biodegradable Polymers.Biomacromolecules · 2026Review
- Yeast-Mediated Plastic Biodegradation.International journal of molecular sciences · 2026Review
- The effect of ionic strength on PETase enzymes: An experimental and computational study.Protein science : a publication of the Protein Society · 2026Article
- Degradation of polyethylene terephthalate by microorganisms and their enzymes: A review of experimental and in silico research.World journal of microbiology & biotechnology · 2025Review
- Unveiling the toxicity of micro-nanoplastics: A systematic exploration of understanding environmental and health implications.Toxicology reports · 2025Review
- Article
- Review
- Opportunities and challenges for plastic depolymerization by biomimetic catalysis.Chemical science · 2024Review
- Discovery and mechanism-guided engineering of BHET hydrolases for improved PET recycling and upcycling.Nature communications · 2023Article
- Enzymatic post-consumer poly(ethylene terephthalate) (PET) depolymerization using commercial enzymes.3 Biotech · 2023Article
- Fungal Screening for Potential PET Depolymerization.Polymers · 2023Article
- Post-Consumer Poly(ethylene terephthalate) (PET) Depolymerization byMolecules (Basel, Switzerland) · 2022Article
- An Overview into Polyethylene Terephthalate (PET) Hydrolases and Efforts in Tailoring Enzymes for Improved Plastic Degradation.International journal of molecular sciences · 2022Review
- Discovery and Genetic Code Expansion of a Polyethylene Terephthalate (PET) Hydrolase from the Human Saliva Metagenome for the Degradation and Bio-Functionalization of PET.Angewandte Chemie (International ed. in English) · 2022Article
- Fungal Enzymes Involved in Plastics Biodegradation.Microorganisms · 2022Review
- Mechanism-Based Design of Efficient PET Hydrolases.ACS catalysis · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Poly(ethylene terephthalate) (PET) is one of the most consumed plastics in the world. The development of efficient technologies for its depolymerization for monomers reuse is highly encouraged, since current recycling rates are still very low. In this study, 16 commercial lipases and cutinases were evaluated for their abilities to catalyze the hydrolysis of two PET samples. Humicola insolens cutinase showed the best performance and was then used in reactions on other PET sources, solely or in combination with the efficient mono(hydroxyethyl terephthalate)-converting lipase from Candida antarctica. Synergy degrees of the final titers of up to 2.2 (i.e., more than double of the concentration when both enzymes were used, as compared to their use alone) were found, with increased terephthalic acid formation rates, reaching a maximum of 59,989 µmol/L (9.36 g/L). These findings open up new possibilities for the conversion of post-consumer PET packages into their minimal monomers, which can be used as drop in at existing industrial facilities.
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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.