ArticleRSC advances2022
A flexible kinetic assay efficiently sorts prospective biocatalysts for PET plastic subunit hydrolysis.
Article in RSC advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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.
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.
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Who cites it
17 citing papers in PubMed, 31 citations in OpenAlex.
- Megascale recombination generates millions of catalytically competent PETases.bioRxiv : the preprint server for biology · 2026Article
- Isosteric Engineering of Enzymes: Overcoming Activity-Stability Trade-Offs by Site-Selective CH → N Substitutions.Angewandte Chemie (International ed. in English) · 2026Article
- A fluorescence-activated droplet sorting assay for ultra-high-throughput screening of PET hydrolases based on a pH indicator.RSC chemical biology · 2026Article
- Production and Evaluation of Fluorophore-Doped Polymer Substrates to Screen for Plastic-Degrading Enzymes.ACS sustainable chemistry & engineering · 2026Article
- Article
- Microbial enzymes for plastic degradation: a comprehensive review of current status and emerging trends.Biodegradation · 2026Review
- The Esterase Gs Derived fromBiology · 2025Article
- Improvement in the Thermal Stability ofMolecules (Basel, Switzerland) · 2025Article
- Efficient Removal of Phenol Red Dye from Polluted Water Using Sustainable Low-Cost Sewage Sludge Activated Carbon: Adsorption and Reusability Studies.Molecules (Basel, Switzerland) · 2024Article
- Increased cytoplasmic expression of PETase enzymes in E. coli.Microbial cell factories · 2024Article
- Enzyme Benchmarking with Polyethylene Furanoate Soluble Scaffolds for Directed Evolution of PEFases.ACS omega · 2024Article
- Understanding the Catalytic Efficiency of Two Polyester Degrading Enzymes: An Experimental and Theoretical Investigation.ACS omega · 2024Article
- A High-Throughput Screening Platform for Engineering Poly(ethylene Terephthalate) Hydrolases.ACS catalysis · 2024Article
- Integration of pH Control into Chi.Bio Reactors and Demonstration with Small-Scale Enzymatic Poly(ethylene terephthalate) Hydrolysis.Biochemistry · 2024Article
- Polyester degradation by soil bacteria: identification of conserved BHETase enzymes in Streptomyces.Communications biology · 2024Article
- Structural and Biochemical Insights into Bis(2-hydroxyethyl) Terephthalate Degrading Carboxylesterase Isolated from Psychrotrophic BacteriumInternational journal of molecular sciences · 2023Article
- Sourcing thermotolerant poly(ethylene terephthalate) hydrolase scaffolds from natural diversity.Nature communications · 2022Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Esterase enzymes catalyze diverse hydrolysis reactions with important biological, commercial, and biotechnological applications. For the improvement of these biocatalysts, there is a need for widely accessible, inexpensive, and adaptable activity screening assays that identify enzymes with particular substrate specificities. Natural systems for biopolymer bioconversion, and likely those designed to mimic them, depend on cocktails of enzymes, each of which specifically targets the intact material as well as water-soluble subunits of varying size. In this work, we have adapted a UV/visible assay using pH-sensitive sulfonphthalein dyes for the real-time quantification of ester hydrolysis of bis-(2-hydroxyethyl) terephthalate (BHET), a subunit of polyethylene terephthalate (PET) plastic. We applied this method to a diverse set of known PET hydrolases and commercial esterases in a microplate format. The approach identified four PET hydrolases and one commercial esterase with high levels of specificity for BHET hydrolysis. Five additional PET hydrolases and three commercial esterases, including a thermophilic enzyme, effectively hydrolyzed both BHET and its monoester product MHET (mono-(2-hydroxyethyl) terephthalate). Specific activities were discernible within one hour and reactions reached an unequivocal endpoint well within 24 hours. The results from the UV/visible method correlated well with conventional HPLC analysis of the reaction products. We examined the suitability of the method toward variable pH, temperature, enzyme preparation method, mono- and multi-ester substrate type, and level of sensitivity
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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.