Search NASA⌕ Search
Home/Archive/DOE OSTI

DOE OSTI · 3600509

Enzymatic Nylon Deconstruction: Enzyme Discovery, Engineering, and Opportunities

Bourgery, Célestin [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)] (ORCID:0000000273182218)·Kato, Dai-ichiro [Kagoshima University (Japan)]·Capra, Nikolas [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)] (ORCID:0000000228986479)·Korey, Matthew [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)]·Qian, Liangyu [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)] (ORCID:0009000212029938)·Negoro, Seiji [University of Hyogo, Himeji (Japan)]·Michener, Joshua K. [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)] (ORCID:0000000323028180)
View original source ↗Read source document ↗Export metadata ↓

Abstract

Nylons are widely used synthetic polyamides valued for their strength, versatility, and durability across diverse applications. However, their petrochemical origin and energy-intensive production underscore the need for efficient, circular solutions. Conventional recycling methods remain limited by incomplete recovery, material degradation, and costly sorting requirements. Enzymatic depolymerization offers a selective, low-energy alternative capable of processing mixed waste streams under mild conditions. While significant progress has been achieved for polyesters, enzymatic degradation of polyamides is still at an early stage. The discovery of nylon hydrolases demonstrated the potential of biological systems to evolve catalysts for synthetic polyamides, yet reported depolymerization yields remain low. These limitations reflect both the structural complexity of nylons and the need for improved enzyme discovery and engineering. In conclusion, this review highlights recent advances, key challenges, and future directions for enzymatic nylon recycling, outlining its potential role enabling mixed polymer waste to be used as a green feedstock for remanufacturing.

Explore related subjects

AmidesOrganic polymersPeptides and proteinsPlasticsRecycling

Keep this discovery

BibTeXRIS

Bourgery, Célestin [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)] (ORCID:0000000273182218), Kato, Dai-ichiro [Kagoshima University (Japan)], Capra, Nikolas [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)] (ORCID:0000000228986479), Korey, Matthew [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)], Qian, Liangyu [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)] (ORCID:0009000212029938), Negoro, Seiji [University of Hyogo, Himeji (Japan)], Michener, Joshua K. [Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)] (ORCID:0000000323028180). 2026-05-04. Enzymatic Nylon Deconstruction: Enzyme Discovery, Engineering, and Opportunities. https://doi.org/10.1021/acsmaterialslett.6c00172

Cite the original work for its findings. Save a collection to share your selection of sources.

Discover connections

Recycling subject

Connections use source metadata and explicit phrase matches, not verified experimental comparisons.

KEEP EXPLORING

Related reports

DOE OSTI2025

Cyclic Peptides for Lanthanide Binding

Lanthanide ions are difficult to separate from one another due to their similar chemical properties. The discovery of lanthanide-binding peptides and proteins in nature has led to an increased interest in the possibility of utilizing the strong binding of peptides to lanthanide ions for their separations; as such, there has been an effort to identify or design peptides with improved lanthanide binding and selectivity toward particular lanthanide ions. Here, in this study, we designed and characterized lanthanide-binding cyclic peptides (LBCPs) with molecular dynamics simulations, electronic structure calculations, and emission spectroscopy. Luminescent decay measurements were done to determine the number of water molecules coordinated to the Eu 3+ ion in Eu-LBCP complexes and compare to the predicted number of water molecules by computation to assess the lanthanide-binding affinity of LBCPs. Measured stability constants show binding of the LBCPs to the Eu 3+ ion with stronger than micromolar affinity. We were able to identify multiple peptides that selectively bind to middle lanthanides. We describe the structural basis of the lanthanide-binding selectivity trend with strongest binding to the middle lanthanides, followed by the heavier lanthanides, and finally to the lighter ions.

ions↗
DOE OSTI2026

Improved Protein Semi-Synthesis Enables Biophysical Studies of Thioamide Destabilization of β-Sheet Interactions

Abstract Thioamides are natural post-translational modifications of the peptide backbone and can be introduced synthetically to probe protein folding or functionalize peptides for translational applications. In this work, we demonstrate that thioamide-containing peptides with C-terminal thioesters can be efficiently generated using Knorr pyrazole activation and used in subsequent native chemical ligation reactions to generate thioamide-containing proteins. We compare this method to acyl azide activation and find that both routes provide similar yields. We also investigate ultrasound-mediated desulfurization of the ligation site cysteine for potential advantages over chemical radical initiators. Scaling up our syntheses allows us to study thioamide perturbations to the β-sheet region of the B1 domain of protein G (GB1) as well as β-strand interactions in amyloid fibrils of the Parkinson’s disease protein α-synuclein. In both contexts, we observe dramatic destabilization of the β-sheet networks, manifested in decreased GB1 thermal stability and altered folding and slowed aggregation of α-synuclein. These findings illustrate the impact that a single atom substitution can have on cooperative hydrogen-bonding networks and prompt future study of both systems.

Yanagawa, Evan S. K. [University of Pennsylvania ,↗
DOE OSTI2026

Revealing Hidden Quinones Through Diagnostic MS² Fragmentation of Peptide–Quinone Adducts

Quinones are redox-active components of natural organic matter that mediate electron transfer and influence biogeochemical processes, but many quinones in pyrogenic organic matter (PyOM) remain unresolved because they ionize poorly by mass spectrometry. Here, we present a peptide-tagging approach to improve detection of cysteine-reactive electrophiles in PyOM, with quinones expected to be a dominant subset based on reaction chemistry and selectivity experiments. A cysteine-containing peptide was used to form Michael-addition adducts, enhancing electrospray ionization and enabling untargeted screening by high-performance liquid chromatography-high-resolution tandem mass spectrometry. The method was benchmarked with five quinone standards and applied to extracts from charred plant material as a discovery-level screen for cysteine-reactive targets. We identified 98 quinone-candidate adducts (mean neutral mass ~603 Da), of which more than 70% were not detectable in native MS1 data. Among formula-assigned features, hidden quinone candidates had median (O+N)/C of 0.391 and normalized oxidation state of carbon of -0.281, consistent with relatively low polarity and low oxidation state. These results reveal a previously inaccessible pool of hidden redox-active compounds in PyOM and provide a framework for prioritizing quinone-like electrophiles for confirmation and incorporation into models of fire-driven biogeochemical cycling.

LC-MS/MS↗