A New PETase from the Human Saliva Metagenome and Its Functional Modification via Genetic Code Expansion in Bacteria

Article Chemistry, Multidisciplinary

Discovery and Genetic Code Expansion of a Polyethylene Terephthalate (PET) Hydrolase from the Human Saliva Metagenome for the Degradation and Bio-Functionalization of PET

Bhumrapee Eiamthong et al.

Summary: We report the discovery of a new PET hydrolase, named MG8, from the human saliva metagenome. MG8 exhibits robust PET degradation activities under different conditions and outperforms other hydrolases in degrading PET. Furthermore, we genetically modified MG8 to serve as a covalent binder for PET functionalization, enabling the attachment of protein cargos to PET and other polyester plastics.

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2022)

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Article Biochemistry & Molecular Biology

Novel putative polyethylene terephthalate (PET) plastic degrading enzymes from the environmental metagenome

Isuru Karunatillaka et al.

Summary: A study investigated a PETase enzyme from environmental samples and its distribution in other bacterial communities, identifying similar homologs in JGI metagenomic datasets through BLAST searches. By verifying the protein sequences and conducting phylogenetic analyses, it confirmed that these proteins are putative PETases, and docking analysis further confirmed their functional assignment.

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2022)

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Article Multidisciplinary Sciences

Machine learning-aided engineering of hydrolases for PET depolymerization

Hongyuan Lu et al.

Summary: Plastic waste is an ecological challenge, and enzymatic degradation offers a potentially green and scalable route for plastic recycling. Engineered PETase shows superior activity in hydrolyzing postconsumer PET, and a closed-loop recycling process is demonstrated.

NATURE (2022)

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Article Chemistry, Physical

Multiple Substrate Binding Mode-Guided Engineering of a Thermophilic PET Hydrolase

Lara Pfaff et al.

Summary: Thermophilic polyester hydrolases (PES-H) play a crucial role in the biocatalytic recycling of synthetic polyester polyethylene terephthalate (PET). By studying the crystal structures of two enzymes derived from metagenomes, researchers gained insights into the mechanism of enzymatic PET hydrolysis. Mutations in key residues resulted in improved hydrolytic activity of certain variants, making them potential candidates for industrial plastic recycling processes.

ACS CATALYSIS (2022)

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Article Chemistry, Physical

Directed evolution of an efficient and thermostable PET depolymerase

Elizabeth L. Bell et al.

Summary: The recent discovery of IsPETase, a hydrolytic enzyme that can degrade polyethylene terephthalate (PET), has sparked interest in using biocatalytic approaches to recycle plastics. In this study, we describe an automated, high-throughput directed evolution platform for engineering polymer degrading enzymes. By applying catalytic activity under elevated temperatures, a thermostable IsPETase variant (HotPETase) was successfully engineered to operate at the industrial processing temperature of PET. This HotPETase enzyme showed improved efficiency in degrading PET compared to previously reported enzymes and could selectively breakdown the PET component of multi-materials.

NATURE CATALYSIS (2022)

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Article Chemistry, Physical

Computational Redesign of a PETase for Plastic Biodegradation under Ambient Condition by the GRAPE Strategy

Yinglu Cui et al.

Summary: This study successfully improved the robustness of PETase through a computational strategy, resulting in the redesign of a variant DuraPETase with significantly elevated melting temperature and enhanced degradation of PET films, as well as complete biodegradation of microplastics at mild temperatures. The design strategy presents opportunities for handling uncollectable PET waste and converting resulting monomers into high-value molecules.

ACS CATALYSIS (2021)

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Article Chemistry, Multidisciplinary

Microbial synthesis of vanillin from waste poly(ethylene terephthalate)

Joanna C. Sadler et al.

Summary: This study reports a novel approach to directly upcycle post-consumer PET waste into valuable vanillin using engineered Escherichia coli. After process optimization, a conversion rate of 79% from terephthalic acid to vanillin was achieved, marking a significant improvement in yield. This work demonstrates the first biological upcycling of post-consumer plastic waste into vanillin, showcasing the potential for sustainable solutions in the plastic recycling industry.

GREEN CHEMISTRY (2021)

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Article Multidisciplinary Sciences