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A New PETase from the Human Saliva Metagenome and Its Functional Modification via Genetic Code Expansion in Bacteria
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Researchers discovered a novel PET-degrading enzyme from the human saliva metagenome that outperforms previously characterized PETases, and demonstrated its functional modification through genetic code expansion to incorporate non-canonical amino acids.
The discovery and engineering of new plastic degrading enzymes is an important challenge in chemical biotechnology to enable transition to a more sustainable and circular plastics economy. This field has so far yielded a range of enzymes and microbial pathways for the recycling and valorization of plastic waste. New research from Uttamapinant et al. reports the discovery of a novel polyethylene terephthalate (PET) hydrolase from the human saliva metagenome that displays improved properties and catalytic performance over previously characterized PET hydrolases (PETases). The authors also demonstrate the site-specific incorporation of a photocaged unnatural amino acid, 2,3-diaminopropionic acid (DAP), which upon photodecaging enables covalent binding of DAP to the PET surface. Thus, this work highlights metagenomic datasets as an untapped source of new PET degrading enzymes and the chemical modification of PETases via genetic code expansion, enabling new biotechnologies for the circular plastics economy.
More Papers Like This
A New PETase from the Human Saliva Metagenome and Its Functional Modification via Genetic Code Expansion in Bacteria
AI summary Read the abstract
Researchers discovered and engineered a new PETase enzyme from human saliva metagenome data, demonstrating its ability to break down PET plastic. Functional modifications improved its catalytic efficiency, contributing to the development of biological tools for plastic recycling.
An Efficient Protein Evolution Workflow for the Improvement of Bacterial PET Hydrolyzing Enzymes.
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Researchers developed a protein engineering workflow to improve bacterial enzymes that degrade PET plastic, combining semi-rational design with high-throughput screening. The resulting engineered enzyme variant achieved over 80% depolymerization of PET nanoparticles within 1.5 hours using only small amounts of enzyme.
Genetic code expansion of plastic-degrading enzymes for detection of microplastics
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Researchers engineered PET-degrading enzymes to create variants that form covalent bonds with PET microplastic particles, enabling enzyme-based detection of microplastics. This proof-of-concept work repurposes plastic-degrading enzymes as analytical detection tools.
An archaeal lid-containing feruloyl-esterase degrades polyethylene terephthalate (PET)
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This study identified the first archaeal enzyme capable of degrading PET plastic, characterizing its structure and biochemical properties. Expanding the diversity of organisms with PET-degrading enzymes could accelerate the development of biological strategies for breaking down the microplastics contaminating marine and terrestrial environments.
Rational Design of Disulfide Bridges in BbPETaseCD for Enhancing the Enzymatic Performance in PET Degradation
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Researchers rationally designed disulfide bridges in BbPETase, a PET-degrading enzyme from a Burkholderiales bacterium, to enhance its thermostability and enzymatic performance, offering a promising avenue for more efficient biological recycling of PET plastic waste.
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When a large batch of papers lands in the Atlas, we read through it and send a short write-up of what stood out.