ArticleChemSusChem2025
Identification of Urethanases for Biocatalytic Recycling of Toluene Diisocyanate- and Methylene Diphenyl Diisocyanate-Based Polyurethanes.
Article in ChemSusChem, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
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Who cites it
3 citing papers in PubMed.
- Advances in amidases and urethanases as depolymerization biocatalysts.Nature chemical biology · 2026Review
- Environmental Identification of Novel Enzymes for Polyurethane and Polyamide Degradation.Angewandte Chemie (International ed. in English) · 2026Article
- The discovery of new metagenomic urethanases utilising a novel colorimetric assay for applications in the biodegradation of polyurethanes.Green chemistry : an international journal and green chemistry resource : GC · 2025Article
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Authors and funding
8 authors.
Funding
Abstract
In this study, the three urethanases TflABH, MthABH, and OspAmd, originating from two distinct enzyme superfamilies, are identified and characterized with respect to their potential in polyurethane (PUR) degradation. The substrate scope included five industrially relevant toluene diisocyanate- and methylene diphenyl diisocyanate-based carbamates with varied alcohol moieties, representative of intermediates from chemical PUR recycling. Notably, TflABH and MthABH are the first urethanases from an esterase superfamily shown to efficiently hydrolyze at least four of the five tested PU-related substrates. Among these, TflABH displayed exceptional thermostability, with a melting temperature (T
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Registered trials
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